data_9GC4
# 
_entry.id   9GC4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GC4         pdb_00009gc4 10.2210/pdb9gc4/pdb 
WWPDB D_1292140733 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-02-12 
2 'Structure model' 1 1 2025-02-26 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GC4 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              david.hargreaves@astrazeneca.com 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Hargreaves 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4441-0039 
# 
_audit_author.name               'Hargreaves, D.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-4441-0039 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                3700 
_citation.page_last                 3748 
_citation.title                     'Highly Optimized CNS Penetrant Inhibitors of EGFR Exon20 Insertion Mutations.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02811 
_citation.pdbx_database_id_PubMed   39869768 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McCoull, W.'              1  ? 
primary 'Thomson, C.'              2  ? 
primary 'Braybrooke, E.'           3  ? 
primary 'Chan, C.'                 4  ? 
primary 'Colclough, N.'            5  ? 
primary 'Cortes Gonzalez, M.A.'    6  ? 
primary 'Cosulich, S.'             7  ? 
primary 'Davies, N.L.'             8  ? 
primary 
;Floc'h, N.
;
9  ? 
primary 'Greenwood, R.'            10 ? 
primary 'Hargreaves, D.'           11 ? 
primary 'Huang, P.'                12 ? 
primary 'Hunt, T.A.'               13 ? 
primary 'Johnson, T.'              14 ? 
primary 'Johnstrom, P.'            15 ? 
primary 'Kettle, J.G.'             16 ? 
primary 'Kondrashov, M.'           17 ? 
primary 'Kostomiris, D.H.'         18 ? 
primary 'Li, S.'                   19 ? 
primary 'Lister, A.'               20 ? 
primary 'Martin, S.'               21 ? 
primary 'McKerrecher, D.'          22 ? 
primary 'McLean, N.'               23 ? 
primary 'Nissink, J.W.M.'          24 ? 
primary 'Orme, J.P.'               25 ? 
primary 'Orwig, P.'                26 ? 
primary 'Packer, M.J.'             27 ? 
primary 'Pearson, S.'              28 ? 
primary 'Qin, L.'                  29 ? 
primary 'Felisberto-Rodrigues, C.' 30 ? 
primary 'Savoca, A.'               31 ? 
primary 'Schou, M.'                32 ? 
primary 'Stokes, S.'               33 ? 
primary 'Swaih, A.M.'              34 ? 
primary 'Talbot, S.'               35 ? 
primary 'Tucker, M.J.'             36 ? 
primary 'Ward, R.A.'               37 ? 
primary 'Wadforth, E.'             38 ? 
primary 'Wang, C.'                 39 ? 
primary 'Wilson, J.'               40 ? 
primary 'Yang, Y.'                 41 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Epidermal growth factor receptor' 37774.594 3   2.7.10.1 ? ? ? 
2 non-polymer syn 
'1-[2-[3-(3-chloranyl-6-fluoranyl-pyridin-2-yl)oxyphenyl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one' 
464.879   2   ?        ? ? ? 
3 water       nat water 18.015    195 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Proto-oncogene c-ErbB-1,Receptor tyrosine-protein kinase erbB-1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPG
NPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQH
VKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKG
ERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDV
VDADEYLIPQQG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPG
NPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQH
VKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKG
ERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDV
VDADEYLIPQQG
;
_entity_poly.pdbx_strand_id                 A,B,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-[2-[3-(3-chloranyl-6-fluoranyl-pyridin-2-yl)oxyphenyl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one' 
A1IZ7 
3 water                                                                                                                           
HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   GLY n 
1 4   GLU n 
1 5   ALA n 
1 6   PRO n 
1 7   ASN n 
1 8   GLN n 
1 9   ALA n 
1 10  LEU n 
1 11  LEU n 
1 12  ARG n 
1 13  ILE n 
1 14  LEU n 
1 15  LYS n 
1 16  GLU n 
1 17  THR n 
1 18  GLU n 
1 19  PHE n 
1 20  LYS n 
1 21  LYS n 
1 22  ILE n 
1 23  LYS n 
1 24  VAL n 
1 25  LEU n 
1 26  GLY n 
1 27  SER n 
1 28  GLY n 
1 29  ALA n 
1 30  PHE n 
1 31  GLY n 
1 32  THR n 
1 33  VAL n 
1 34  TYR n 
1 35  LYS n 
1 36  GLY n 
1 37  LEU n 
1 38  TRP n 
1 39  ILE n 
1 40  PRO n 
1 41  GLU n 
1 42  GLY n 
1 43  GLU n 
1 44  LYS n 
1 45  VAL n 
1 46  LYS n 
1 47  ILE n 
1 48  PRO n 
1 49  VAL n 
1 50  ALA n 
1 51  ILE n 
1 52  LYS n 
1 53  GLU n 
1 54  LEU n 
1 55  ARG n 
1 56  GLU n 
1 57  ALA n 
1 58  THR n 
1 59  SER n 
1 60  PRO n 
1 61  LYS n 
1 62  ALA n 
1 63  ASN n 
1 64  LYS n 
1 65  GLU n 
1 66  ILE n 
1 67  LEU n 
1 68  ASP n 
1 69  GLU n 
1 70  ALA n 
1 71  TYR n 
1 72  VAL n 
1 73  MET n 
1 74  ALA n 
1 75  SER n 
1 76  VAL n 
1 77  ASP n 
1 78  ASN n 
1 79  PRO n 
1 80  GLY n 
1 81  ASN n 
1 82  PRO n 
1 83  HIS n 
1 84  VAL n 
1 85  CYS n 
1 86  ARG n 
1 87  LEU n 
1 88  LEU n 
1 89  GLY n 
1 90  ILE n 
1 91  CYS n 
1 92  LEU n 
1 93  THR n 
1 94  SER n 
1 95  THR n 
1 96  VAL n 
1 97  GLN n 
1 98  LEU n 
1 99  ILE n 
1 100 THR n 
1 101 GLN n 
1 102 LEU n 
1 103 MET n 
1 104 PRO n 
1 105 PHE n 
1 106 GLY n 
1 107 CYS n 
1 108 LEU n 
1 109 LEU n 
1 110 ASP n 
1 111 TYR n 
1 112 VAL n 
1 113 ARG n 
1 114 GLU n 
1 115 HIS n 
1 116 LYS n 
1 117 ASP n 
1 118 ASN n 
1 119 ILE n 
1 120 GLY n 
1 121 SER n 
1 122 GLN n 
1 123 TYR n 
1 124 LEU n 
1 125 LEU n 
1 126 ASN n 
1 127 TRP n 
1 128 CYS n 
1 129 VAL n 
1 130 GLN n 
1 131 ILE n 
1 132 ALA n 
1 133 LYS n 
1 134 GLY n 
1 135 MET n 
1 136 ASN n 
1 137 TYR n 
1 138 LEU n 
1 139 GLU n 
1 140 ASP n 
1 141 ARG n 
1 142 ARG n 
1 143 LEU n 
1 144 VAL n 
1 145 HIS n 
1 146 ARG n 
1 147 ASP n 
1 148 LEU n 
1 149 ALA n 
1 150 ALA n 
1 151 ARG n 
1 152 ASN n 
1 153 VAL n 
1 154 LEU n 
1 155 VAL n 
1 156 LYS n 
1 157 THR n 
1 158 PRO n 
1 159 GLN n 
1 160 HIS n 
1 161 VAL n 
1 162 LYS n 
1 163 ILE n 
1 164 THR n 
1 165 ASP n 
1 166 PHE n 
1 167 GLY n 
1 168 LEU n 
1 169 ALA n 
1 170 LYS n 
1 171 LEU n 
1 172 LEU n 
1 173 GLY n 
1 174 ALA n 
1 175 GLU n 
1 176 GLU n 
1 177 LYS n 
1 178 GLU n 
1 179 TYR n 
1 180 HIS n 
1 181 ALA n 
1 182 GLU n 
1 183 GLY n 
1 184 GLY n 
1 185 LYS n 
1 186 VAL n 
1 187 PRO n 
1 188 ILE n 
1 189 LYS n 
1 190 TRP n 
1 191 MET n 
1 192 ALA n 
1 193 LEU n 
1 194 GLU n 
1 195 SER n 
1 196 ILE n 
1 197 LEU n 
1 198 HIS n 
1 199 ARG n 
1 200 ILE n 
1 201 TYR n 
1 202 THR n 
1 203 HIS n 
1 204 GLN n 
1 205 SER n 
1 206 ASP n 
1 207 VAL n 
1 208 TRP n 
1 209 SER n 
1 210 TYR n 
1 211 GLY n 
1 212 VAL n 
1 213 THR n 
1 214 VAL n 
1 215 TRP n 
1 216 GLU n 
1 217 LEU n 
1 218 MET n 
1 219 THR n 
1 220 PHE n 
1 221 GLY n 
1 222 SER n 
1 223 LYS n 
1 224 PRO n 
1 225 TYR n 
1 226 ASP n 
1 227 GLY n 
1 228 ILE n 
1 229 PRO n 
1 230 ALA n 
1 231 SER n 
1 232 GLU n 
1 233 ILE n 
1 234 SER n 
1 235 SER n 
1 236 ILE n 
1 237 LEU n 
1 238 GLU n 
1 239 LYS n 
1 240 GLY n 
1 241 GLU n 
1 242 ARG n 
1 243 LEU n 
1 244 PRO n 
1 245 GLN n 
1 246 PRO n 
1 247 PRO n 
1 248 ILE n 
1 249 CYS n 
1 250 THR n 
1 251 ILE n 
1 252 ASP n 
1 253 VAL n 
1 254 TYR n 
1 255 MET n 
1 256 ILE n 
1 257 MET n 
1 258 ARG n 
1 259 LYS n 
1 260 CYS n 
1 261 TRP n 
1 262 MET n 
1 263 ILE n 
1 264 ASP n 
1 265 ALA n 
1 266 ASP n 
1 267 SER n 
1 268 ARG n 
1 269 PRO n 
1 270 LYS n 
1 271 PHE n 
1 272 ARG n 
1 273 GLU n 
1 274 LEU n 
1 275 ILE n 
1 276 ILE n 
1 277 GLU n 
1 278 PHE n 
1 279 SER n 
1 280 LYS n 
1 281 MET n 
1 282 ALA n 
1 283 ARG n 
1 284 ASP n 
1 285 PRO n 
1 286 GLN n 
1 287 ARG n 
1 288 TYR n 
1 289 LEU n 
1 290 VAL n 
1 291 ILE n 
1 292 GLN n 
1 293 GLY n 
1 294 ASP n 
1 295 GLU n 
1 296 ARG n 
1 297 MET n 
1 298 HIS n 
1 299 LEU n 
1 300 PRO n 
1 301 SER n 
1 302 PRO n 
1 303 THR n 
1 304 ASP n 
1 305 SER n 
1 306 ASN n 
1 307 PHE n 
1 308 TYR n 
1 309 ARG n 
1 310 ALA n 
1 311 LEU n 
1 312 MET n 
1 313 ASP n 
1 314 GLU n 
1 315 GLU n 
1 316 ASP n 
1 317 MET n 
1 318 ASP n 
1 319 ASP n 
1 320 VAL n 
1 321 VAL n 
1 322 ASP n 
1 323 ALA n 
1 324 ASP n 
1 325 GLU n 
1 326 TYR n 
1 327 LEU n 
1 328 ILE n 
1 329 PRO n 
1 330 GLN n 
1 331 GLN n 
1 332 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   332 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'EGFR, ERBB, ERBB1, HER1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IZ7 non-polymer         . 
'1-[2-[3-(3-chloranyl-6-fluoranyl-pyridin-2-yl)oxyphenyl]-3-pyrimidin-4-yl-4,6-dihydropyrrolo[3,4-d]imidazol-5-yl]propan-1-one' ? 
'C23 H18 Cl F N6 O2' 464.879 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'       121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER ? 'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   694  ?    ?   ?   A . n 
A 1 2   SER 2   695  ?    ?   ?   A . n 
A 1 3   GLY 3   696  ?    ?   ?   A . n 
A 1 4   GLU 4   697  ?    ?   ?   A . n 
A 1 5   ALA 5   698  ?    ?   ?   A . n 
A 1 6   PRO 6   699  ?    ?   ?   A . n 
A 1 7   ASN 7   700  ?    ?   ?   A . n 
A 1 8   GLN 8   701  ?    ?   ?   A . n 
A 1 9   ALA 9   702  ?    ?   ?   A . n 
A 1 10  LEU 10  703  703  LEU LEU A . n 
A 1 11  LEU 11  704  704  LEU LEU A . n 
A 1 12  ARG 12  705  705  ARG ARG A . n 
A 1 13  ILE 13  706  706  ILE ILE A . n 
A 1 14  LEU 14  707  707  LEU LEU A . n 
A 1 15  LYS 15  708  708  LYS LYS A . n 
A 1 16  GLU 16  709  709  GLU GLU A . n 
A 1 17  THR 17  710  710  THR THR A . n 
A 1 18  GLU 18  711  711  GLU GLU A . n 
A 1 19  PHE 19  712  712  PHE PHE A . n 
A 1 20  LYS 20  713  713  LYS LYS A . n 
A 1 21  LYS 21  714  714  LYS LYS A . n 
A 1 22  ILE 22  715  715  ILE ILE A . n 
A 1 23  LYS 23  716  716  LYS LYS A . n 
A 1 24  VAL 24  717  717  VAL VAL A . n 
A 1 25  LEU 25  718  718  LEU LEU A . n 
A 1 26  GLY 26  719  719  GLY GLY A . n 
A 1 27  SER 27  720  720  SER SER A . n 
A 1 28  GLY 28  721  721  GLY GLY A . n 
A 1 29  ALA 29  722  722  ALA ALA A . n 
A 1 30  PHE 30  723  723  PHE PHE A . n 
A 1 31  GLY 31  724  724  GLY GLY A . n 
A 1 32  THR 32  725  725  THR THR A . n 
A 1 33  VAL 33  726  726  VAL VAL A . n 
A 1 34  TYR 34  727  727  TYR TYR A . n 
A 1 35  LYS 35  728  728  LYS LYS A . n 
A 1 36  GLY 36  729  729  GLY GLY A . n 
A 1 37  LEU 37  730  730  LEU LEU A . n 
A 1 38  TRP 38  731  731  TRP TRP A . n 
A 1 39  ILE 39  732  732  ILE ILE A . n 
A 1 40  PRO 40  733  733  PRO PRO A . n 
A 1 41  GLU 41  734  734  GLU GLU A . n 
A 1 42  GLY 42  735  735  GLY GLY A . n 
A 1 43  GLU 43  736  736  GLU GLU A . n 
A 1 44  LYS 44  737  737  LYS LYS A . n 
A 1 45  VAL 45  738  738  VAL VAL A . n 
A 1 46  LYS 46  739  739  LYS LYS A . n 
A 1 47  ILE 47  740  740  ILE ILE A . n 
A 1 48  PRO 48  741  741  PRO PRO A . n 
A 1 49  VAL 49  742  742  VAL VAL A . n 
A 1 50  ALA 50  743  743  ALA ALA A . n 
A 1 51  ILE 51  744  744  ILE ILE A . n 
A 1 52  LYS 52  745  745  LYS LYS A . n 
A 1 53  GLU 53  746  746  GLU GLU A . n 
A 1 54  LEU 54  747  747  LEU LEU A . n 
A 1 55  ARG 55  748  748  ARG ARG A . n 
A 1 56  GLU 56  749  749  GLU GLU A . n 
A 1 57  ALA 57  750  750  ALA ALA A . n 
A 1 58  THR 58  751  751  THR THR A . n 
A 1 59  SER 59  752  752  SER SER A . n 
A 1 60  PRO 60  753  753  PRO PRO A . n 
A 1 61  LYS 61  754  754  LYS LYS A . n 
A 1 62  ALA 62  755  755  ALA ALA A . n 
A 1 63  ASN 63  756  756  ASN ASN A . n 
A 1 64  LYS 64  757  757  LYS LYS A . n 
A 1 65  GLU 65  758  758  GLU GLU A . n 
A 1 66  ILE 66  759  759  ILE ILE A . n 
A 1 67  LEU 67  760  760  LEU LEU A . n 
A 1 68  ASP 68  761  761  ASP ASP A . n 
A 1 69  GLU 69  762  762  GLU GLU A . n 
A 1 70  ALA 70  763  763  ALA ALA A . n 
A 1 71  TYR 71  764  764  TYR TYR A . n 
A 1 72  VAL 72  765  765  VAL VAL A . n 
A 1 73  MET 73  766  766  MET MET A . n 
A 1 74  ALA 74  767  767  ALA ALA A . n 
A 1 75  SER 75  768  768  SER SER A . n 
A 1 76  VAL 76  769  769  VAL VAL A . n 
A 1 77  ASP 77  770  770  ASP ASP A . n 
A 1 78  ASN 78  771  771  ASN ASN A . n 
A 1 79  PRO 79  772  772  PRO PRO A . n 
A 1 80  GLY 80  773  773  GLY GLY A . n 
A 1 81  ASN 81  774  774  ASN ASN A . n 
A 1 82  PRO 82  775  775  PRO PRO A . n 
A 1 83  HIS 83  776  776  HIS HIS A . n 
A 1 84  VAL 84  777  777  VAL VAL A . n 
A 1 85  CYS 85  778  778  CYS CYS A . n 
A 1 86  ARG 86  779  779  ARG ARG A . n 
A 1 87  LEU 87  780  780  LEU LEU A . n 
A 1 88  LEU 88  781  781  LEU LEU A . n 
A 1 89  GLY 89  782  782  GLY GLY A . n 
A 1 90  ILE 90  783  783  ILE ILE A . n 
A 1 91  CYS 91  784  784  CYS CYS A . n 
A 1 92  LEU 92  785  785  LEU LEU A . n 
A 1 93  THR 93  786  786  THR THR A . n 
A 1 94  SER 94  787  787  SER SER A . n 
A 1 95  THR 95  788  788  THR THR A . n 
A 1 96  VAL 96  789  789  VAL VAL A . n 
A 1 97  GLN 97  790  790  GLN GLN A . n 
A 1 98  LEU 98  791  791  LEU LEU A . n 
A 1 99  ILE 99  792  792  ILE ILE A . n 
A 1 100 THR 100 793  793  THR THR A . n 
A 1 101 GLN 101 794  794  GLN GLN A . n 
A 1 102 LEU 102 795  795  LEU LEU A . n 
A 1 103 MET 103 796  796  MET MET A . n 
A 1 104 PRO 104 797  797  PRO PRO A . n 
A 1 105 PHE 105 798  798  PHE PHE A . n 
A 1 106 GLY 106 799  799  GLY GLY A . n 
A 1 107 CYS 107 800  800  CYS CYS A . n 
A 1 108 LEU 108 801  801  LEU LEU A . n 
A 1 109 LEU 109 802  802  LEU LEU A . n 
A 1 110 ASP 110 803  803  ASP ASP A . n 
A 1 111 TYR 111 804  804  TYR TYR A . n 
A 1 112 VAL 112 805  805  VAL VAL A . n 
A 1 113 ARG 113 806  806  ARG ARG A . n 
A 1 114 GLU 114 807  807  GLU GLU A . n 
A 1 115 HIS 115 808  808  HIS HIS A . n 
A 1 116 LYS 116 809  809  LYS LYS A . n 
A 1 117 ASP 117 810  810  ASP ASP A . n 
A 1 118 ASN 118 811  811  ASN ASN A . n 
A 1 119 ILE 119 812  812  ILE ILE A . n 
A 1 120 GLY 120 813  813  GLY GLY A . n 
A 1 121 SER 121 814  814  SER SER A . n 
A 1 122 GLN 122 815  815  GLN GLN A . n 
A 1 123 TYR 123 816  816  TYR TYR A . n 
A 1 124 LEU 124 817  817  LEU LEU A . n 
A 1 125 LEU 125 818  818  LEU LEU A . n 
A 1 126 ASN 126 819  819  ASN ASN A . n 
A 1 127 TRP 127 820  820  TRP TRP A . n 
A 1 128 CYS 128 821  821  CYS CYS A . n 
A 1 129 VAL 129 822  822  VAL VAL A . n 
A 1 130 GLN 130 823  823  GLN GLN A . n 
A 1 131 ILE 131 824  824  ILE ILE A . n 
A 1 132 ALA 132 825  825  ALA ALA A . n 
A 1 133 LYS 133 826  826  LYS LYS A . n 
A 1 134 GLY 134 827  827  GLY GLY A . n 
A 1 135 MET 135 828  828  MET MET A . n 
A 1 136 ASN 136 829  829  ASN ASN A . n 
A 1 137 TYR 137 830  830  TYR TYR A . n 
A 1 138 LEU 138 831  831  LEU LEU A . n 
A 1 139 GLU 139 832  832  GLU GLU A . n 
A 1 140 ASP 140 833  833  ASP ASP A . n 
A 1 141 ARG 141 834  834  ARG ARG A . n 
A 1 142 ARG 142 835  835  ARG ARG A . n 
A 1 143 LEU 143 836  836  LEU LEU A . n 
A 1 144 VAL 144 837  837  VAL VAL A . n 
A 1 145 HIS 145 838  838  HIS HIS A . n 
A 1 146 ARG 146 839  839  ARG ARG A . n 
A 1 147 ASP 147 840  840  ASP ASP A . n 
A 1 148 LEU 148 841  841  LEU LEU A . n 
A 1 149 ALA 149 842  842  ALA ALA A . n 
A 1 150 ALA 150 843  843  ALA ALA A . n 
A 1 151 ARG 151 844  844  ARG ARG A . n 
A 1 152 ASN 152 845  845  ASN ASN A . n 
A 1 153 VAL 153 846  846  VAL VAL A . n 
A 1 154 LEU 154 847  847  LEU LEU A . n 
A 1 155 VAL 155 848  848  VAL VAL A . n 
A 1 156 LYS 156 849  849  LYS LYS A . n 
A 1 157 THR 157 850  850  THR THR A . n 
A 1 158 PRO 158 851  851  PRO PRO A . n 
A 1 159 GLN 159 852  852  GLN GLN A . n 
A 1 160 HIS 160 853  853  HIS HIS A . n 
A 1 161 VAL 161 854  854  VAL VAL A . n 
A 1 162 LYS 162 855  855  LYS LYS A . n 
A 1 163 ILE 163 856  856  ILE ILE A . n 
A 1 164 THR 164 857  857  THR THR A . n 
A 1 165 ASP 165 858  858  ASP ASP A . n 
A 1 166 PHE 166 859  859  PHE PHE A . n 
A 1 167 GLY 167 860  860  GLY GLY A . n 
A 1 168 LEU 168 861  861  LEU LEU A . n 
A 1 169 ALA 169 862  862  ALA ALA A . n 
A 1 170 LYS 170 863  863  LYS LYS A . n 
A 1 171 LEU 171 864  864  LEU LEU A . n 
A 1 172 LEU 172 865  865  LEU LEU A . n 
A 1 173 GLY 173 866  866  GLY GLY A . n 
A 1 174 ALA 174 867  867  ALA ALA A . n 
A 1 175 GLU 175 868  868  GLU GLU A . n 
A 1 176 GLU 176 869  869  GLU GLU A . n 
A 1 177 LYS 177 870  870  LYS LYS A . n 
A 1 178 GLU 178 871  871  GLU GLU A . n 
A 1 179 TYR 179 872  872  TYR TYR A . n 
A 1 180 HIS 180 873  873  HIS HIS A . n 
A 1 181 ALA 181 874  874  ALA ALA A . n 
A 1 182 GLU 182 875  875  GLU GLU A . n 
A 1 183 GLY 183 876  876  GLY GLY A . n 
A 1 184 GLY 184 877  877  GLY GLY A . n 
A 1 185 LYS 185 878  878  LYS LYS A . n 
A 1 186 VAL 186 879  879  VAL VAL A . n 
A 1 187 PRO 187 880  880  PRO PRO A . n 
A 1 188 ILE 188 881  881  ILE ILE A . n 
A 1 189 LYS 189 882  882  LYS LYS A . n 
A 1 190 TRP 190 883  883  TRP TRP A . n 
A 1 191 MET 191 884  884  MET MET A . n 
A 1 192 ALA 192 885  885  ALA ALA A . n 
A 1 193 LEU 193 886  886  LEU LEU A . n 
A 1 194 GLU 194 887  887  GLU GLU A . n 
A 1 195 SER 195 888  888  SER SER A . n 
A 1 196 ILE 196 889  889  ILE ILE A . n 
A 1 197 LEU 197 890  890  LEU LEU A . n 
A 1 198 HIS 198 891  891  HIS HIS A . n 
A 1 199 ARG 199 892  892  ARG ARG A . n 
A 1 200 ILE 200 893  893  ILE ILE A . n 
A 1 201 TYR 201 894  894  TYR TYR A . n 
A 1 202 THR 202 895  895  THR THR A . n 
A 1 203 HIS 203 896  896  HIS HIS A . n 
A 1 204 GLN 204 897  897  GLN GLN A . n 
A 1 205 SER 205 898  898  SER SER A . n 
A 1 206 ASP 206 899  899  ASP ASP A . n 
A 1 207 VAL 207 900  900  VAL VAL A . n 
A 1 208 TRP 208 901  901  TRP TRP A . n 
A 1 209 SER 209 902  902  SER SER A . n 
A 1 210 TYR 210 903  903  TYR TYR A . n 
A 1 211 GLY 211 904  904  GLY GLY A . n 
A 1 212 VAL 212 905  905  VAL VAL A . n 
A 1 213 THR 213 906  906  THR THR A . n 
A 1 214 VAL 214 907  907  VAL VAL A . n 
A 1 215 TRP 215 908  908  TRP TRP A . n 
A 1 216 GLU 216 909  909  GLU GLU A . n 
A 1 217 LEU 217 910  910  LEU LEU A . n 
A 1 218 MET 218 911  911  MET MET A . n 
A 1 219 THR 219 912  912  THR THR A . n 
A 1 220 PHE 220 913  913  PHE PHE A . n 
A 1 221 GLY 221 914  914  GLY GLY A . n 
A 1 222 SER 222 915  915  SER SER A . n 
A 1 223 LYS 223 916  916  LYS LYS A . n 
A 1 224 PRO 224 917  917  PRO PRO A . n 
A 1 225 TYR 225 918  918  TYR TYR A . n 
A 1 226 ASP 226 919  919  ASP ASP A . n 
A 1 227 GLY 227 920  920  GLY GLY A . n 
A 1 228 ILE 228 921  921  ILE ILE A . n 
A 1 229 PRO 229 922  922  PRO PRO A . n 
A 1 230 ALA 230 923  923  ALA ALA A . n 
A 1 231 SER 231 924  924  SER SER A . n 
A 1 232 GLU 232 925  925  GLU GLU A . n 
A 1 233 ILE 233 926  926  ILE ILE A . n 
A 1 234 SER 234 927  927  SER SER A . n 
A 1 235 SER 235 928  928  SER SER A . n 
A 1 236 ILE 236 929  929  ILE ILE A . n 
A 1 237 LEU 237 930  930  LEU LEU A . n 
A 1 238 GLU 238 931  931  GLU GLU A . n 
A 1 239 LYS 239 932  932  LYS LYS A . n 
A 1 240 GLY 240 933  933  GLY GLY A . n 
A 1 241 GLU 241 934  934  GLU GLU A . n 
A 1 242 ARG 242 935  935  ARG ARG A . n 
A 1 243 LEU 243 936  936  LEU LEU A . n 
A 1 244 PRO 244 937  937  PRO PRO A . n 
A 1 245 GLN 245 938  938  GLN GLN A . n 
A 1 246 PRO 246 939  939  PRO PRO A . n 
A 1 247 PRO 247 940  940  PRO PRO A . n 
A 1 248 ILE 248 941  941  ILE ILE A . n 
A 1 249 CYS 249 942  942  CYS CYS A . n 
A 1 250 THR 250 943  943  THR THR A . n 
A 1 251 ILE 251 944  944  ILE ILE A . n 
A 1 252 ASP 252 945  945  ASP ASP A . n 
A 1 253 VAL 253 946  946  VAL VAL A . n 
A 1 254 TYR 254 947  947  TYR TYR A . n 
A 1 255 MET 255 948  948  MET MET A . n 
A 1 256 ILE 256 949  949  ILE ILE A . n 
A 1 257 MET 257 950  950  MET MET A . n 
A 1 258 ARG 258 951  951  ARG ARG A . n 
A 1 259 LYS 259 952  952  LYS LYS A . n 
A 1 260 CYS 260 953  953  CYS CYS A . n 
A 1 261 TRP 261 954  954  TRP TRP A . n 
A 1 262 MET 262 955  955  MET MET A . n 
A 1 263 ILE 263 956  956  ILE ILE A . n 
A 1 264 ASP 264 957  957  ASP ASP A . n 
A 1 265 ALA 265 958  958  ALA ALA A . n 
A 1 266 ASP 266 959  959  ASP ASP A . n 
A 1 267 SER 267 960  960  SER SER A . n 
A 1 268 ARG 268 961  961  ARG ARG A . n 
A 1 269 PRO 269 962  962  PRO PRO A . n 
A 1 270 LYS 270 963  963  LYS LYS A . n 
A 1 271 PHE 271 964  964  PHE PHE A . n 
A 1 272 ARG 272 965  965  ARG ARG A . n 
A 1 273 GLU 273 966  966  GLU GLU A . n 
A 1 274 LEU 274 967  967  LEU LEU A . n 
A 1 275 ILE 275 968  968  ILE ILE A . n 
A 1 276 ILE 276 969  969  ILE ILE A . n 
A 1 277 GLU 277 970  970  GLU GLU A . n 
A 1 278 PHE 278 971  971  PHE PHE A . n 
A 1 279 SER 279 972  972  SER SER A . n 
A 1 280 LYS 280 973  973  LYS LYS A . n 
A 1 281 MET 281 974  974  MET MET A . n 
A 1 282 ALA 282 975  975  ALA ALA A . n 
A 1 283 ARG 283 976  976  ARG ARG A . n 
A 1 284 ASP 284 977  977  ASP ASP A . n 
A 1 285 PRO 285 978  978  PRO PRO A . n 
A 1 286 GLN 286 979  979  GLN GLN A . n 
A 1 287 ARG 287 980  980  ARG ARG A . n 
A 1 288 TYR 288 981  981  TYR TYR A . n 
A 1 289 LEU 289 982  982  LEU LEU A . n 
A 1 290 VAL 290 983  983  VAL VAL A . n 
A 1 291 ILE 291 984  984  ILE ILE A . n 
A 1 292 GLN 292 985  985  GLN GLN A . n 
A 1 293 GLY 293 986  986  GLY GLY A . n 
A 1 294 ASP 294 987  987  ASP ASP A . n 
A 1 295 GLU 295 988  ?    ?   ?   A . n 
A 1 296 ARG 296 989  ?    ?   ?   A . n 
A 1 297 MET 297 990  ?    ?   ?   A . n 
A 1 298 HIS 298 991  ?    ?   ?   A . n 
A 1 299 LEU 299 992  ?    ?   ?   A . n 
A 1 300 PRO 300 993  ?    ?   ?   A . n 
A 1 301 SER 301 994  ?    ?   ?   A . n 
A 1 302 PRO 302 995  ?    ?   ?   A . n 
A 1 303 THR 303 996  ?    ?   ?   A . n 
A 1 304 ASP 304 997  ?    ?   ?   A . n 
A 1 305 SER 305 998  ?    ?   ?   A . n 
A 1 306 ASN 306 999  ?    ?   ?   A . n 
A 1 307 PHE 307 1000 ?    ?   ?   A . n 
A 1 308 TYR 308 1001 ?    ?   ?   A . n 
A 1 309 ARG 309 1002 ?    ?   ?   A . n 
A 1 310 ALA 310 1003 ?    ?   ?   A . n 
A 1 311 LEU 311 1004 ?    ?   ?   A . n 
A 1 312 MET 312 1005 ?    ?   ?   A . n 
A 1 313 ASP 313 1006 ?    ?   ?   A . n 
A 1 314 GLU 314 1007 ?    ?   ?   A . n 
A 1 315 GLU 315 1008 ?    ?   ?   A . n 
A 1 316 ASP 316 1009 ?    ?   ?   A . n 
A 1 317 MET 317 1010 ?    ?   ?   A . n 
A 1 318 ASP 318 1011 ?    ?   ?   A . n 
A 1 319 ASP 319 1012 ?    ?   ?   A . n 
A 1 320 VAL 320 1013 ?    ?   ?   A . n 
A 1 321 VAL 321 1014 ?    ?   ?   A . n 
A 1 322 ASP 322 1015 ?    ?   ?   A . n 
A 1 323 ALA 323 1016 ?    ?   ?   A . n 
A 1 324 ASP 324 1017 ?    ?   ?   A . n 
A 1 325 GLU 325 1018 ?    ?   ?   A . n 
A 1 326 TYR 326 1019 ?    ?   ?   A . n 
A 1 327 LEU 327 1020 ?    ?   ?   A . n 
A 1 328 ILE 328 1021 ?    ?   ?   A . n 
A 1 329 PRO 329 1022 ?    ?   ?   A . n 
A 1 330 GLN 330 1023 ?    ?   ?   A . n 
A 1 331 GLN 331 1024 ?    ?   ?   A . n 
A 1 332 GLY 332 1025 ?    ?   ?   A . n 
B 1 1   GLY 1   694  ?    ?   ?   B . n 
B 1 2   SER 2   695  ?    ?   ?   B . n 
B 1 3   GLY 3   696  ?    ?   ?   B . n 
B 1 4   GLU 4   697  ?    ?   ?   B . n 
B 1 5   ALA 5   698  ?    ?   ?   B . n 
B 1 6   PRO 6   699  ?    ?   ?   B . n 
B 1 7   ASN 7   700  ?    ?   ?   B . n 
B 1 8   GLN 8   701  ?    ?   ?   B . n 
B 1 9   ALA 9   702  ?    ?   ?   B . n 
B 1 10  LEU 10  703  703  LEU LEU B . n 
B 1 11  LEU 11  704  704  LEU LEU B . n 
B 1 12  ARG 12  705  705  ARG ARG B . n 
B 1 13  ILE 13  706  706  ILE ILE B . n 
B 1 14  LEU 14  707  707  LEU LEU B . n 
B 1 15  LYS 15  708  708  LYS LYS B . n 
B 1 16  GLU 16  709  709  GLU GLU B . n 
B 1 17  THR 17  710  710  THR THR B . n 
B 1 18  GLU 18  711  711  GLU GLU B . n 
B 1 19  PHE 19  712  712  PHE PHE B . n 
B 1 20  LYS 20  713  713  LYS LYS B . n 
B 1 21  LYS 21  714  714  LYS LYS B . n 
B 1 22  ILE 22  715  715  ILE ILE B . n 
B 1 23  LYS 23  716  716  LYS LYS B . n 
B 1 24  VAL 24  717  717  VAL VAL B . n 
B 1 25  LEU 25  718  718  LEU LEU B . n 
B 1 26  GLY 26  719  719  GLY GLY B . n 
B 1 27  SER 27  720  720  SER SER B . n 
B 1 28  GLY 28  721  721  GLY GLY B . n 
B 1 29  ALA 29  722  722  ALA ALA B . n 
B 1 30  PHE 30  723  723  PHE PHE B . n 
B 1 31  GLY 31  724  724  GLY GLY B . n 
B 1 32  THR 32  725  725  THR THR B . n 
B 1 33  VAL 33  726  726  VAL VAL B . n 
B 1 34  TYR 34  727  727  TYR TYR B . n 
B 1 35  LYS 35  728  728  LYS LYS B . n 
B 1 36  GLY 36  729  729  GLY GLY B . n 
B 1 37  LEU 37  730  730  LEU LEU B . n 
B 1 38  TRP 38  731  731  TRP TRP B . n 
B 1 39  ILE 39  732  732  ILE ILE B . n 
B 1 40  PRO 40  733  733  PRO PRO B . n 
B 1 41  GLU 41  734  734  GLU GLU B . n 
B 1 42  GLY 42  735  735  GLY GLY B . n 
B 1 43  GLU 43  736  736  GLU GLU B . n 
B 1 44  LYS 44  737  737  LYS LYS B . n 
B 1 45  VAL 45  738  738  VAL VAL B . n 
B 1 46  LYS 46  739  739  LYS LYS B . n 
B 1 47  ILE 47  740  740  ILE ILE B . n 
B 1 48  PRO 48  741  741  PRO PRO B . n 
B 1 49  VAL 49  742  742  VAL VAL B . n 
B 1 50  ALA 50  743  743  ALA ALA B . n 
B 1 51  ILE 51  744  744  ILE ILE B . n 
B 1 52  LYS 52  745  745  LYS LYS B . n 
B 1 53  GLU 53  746  746  GLU GLU B . n 
B 1 54  LEU 54  747  747  LEU LEU B . n 
B 1 55  ARG 55  748  748  ARG ARG B . n 
B 1 56  GLU 56  749  749  GLU GLU B . n 
B 1 57  ALA 57  750  750  ALA ALA B . n 
B 1 58  THR 58  751  751  THR THR B . n 
B 1 59  SER 59  752  752  SER SER B . n 
B 1 60  PRO 60  753  753  PRO PRO B . n 
B 1 61  LYS 61  754  754  LYS LYS B . n 
B 1 62  ALA 62  755  755  ALA ALA B . n 
B 1 63  ASN 63  756  756  ASN ASN B . n 
B 1 64  LYS 64  757  757  LYS LYS B . n 
B 1 65  GLU 65  758  758  GLU GLU B . n 
B 1 66  ILE 66  759  759  ILE ILE B . n 
B 1 67  LEU 67  760  760  LEU LEU B . n 
B 1 68  ASP 68  761  761  ASP ASP B . n 
B 1 69  GLU 69  762  762  GLU GLU B . n 
B 1 70  ALA 70  763  763  ALA ALA B . n 
B 1 71  TYR 71  764  764  TYR TYR B . n 
B 1 72  VAL 72  765  765  VAL VAL B . n 
B 1 73  MET 73  766  766  MET MET B . n 
B 1 74  ALA 74  767  767  ALA ALA B . n 
B 1 75  SER 75  768  768  SER SER B . n 
B 1 76  VAL 76  769  769  VAL VAL B . n 
B 1 77  ASP 77  770  770  ASP ASP B . n 
B 1 78  ASN 78  771  771  ASN ASN B . n 
B 1 79  PRO 79  772  772  PRO PRO B . n 
B 1 80  GLY 80  773  773  GLY GLY B . n 
B 1 81  ASN 81  774  774  ASN ASN B . n 
B 1 82  PRO 82  775  775  PRO PRO B . n 
B 1 83  HIS 83  776  776  HIS HIS B . n 
B 1 84  VAL 84  777  777  VAL VAL B . n 
B 1 85  CYS 85  778  778  CYS CYS B . n 
B 1 86  ARG 86  779  779  ARG ARG B . n 
B 1 87  LEU 87  780  780  LEU LEU B . n 
B 1 88  LEU 88  781  781  LEU LEU B . n 
B 1 89  GLY 89  782  782  GLY GLY B . n 
B 1 90  ILE 90  783  783  ILE ILE B . n 
B 1 91  CYS 91  784  784  CYS CYS B . n 
B 1 92  LEU 92  785  785  LEU LEU B . n 
B 1 93  THR 93  786  786  THR THR B . n 
B 1 94  SER 94  787  787  SER SER B . n 
B 1 95  THR 95  788  788  THR THR B . n 
B 1 96  VAL 96  789  789  VAL VAL B . n 
B 1 97  GLN 97  790  790  GLN GLN B . n 
B 1 98  LEU 98  791  791  LEU LEU B . n 
B 1 99  ILE 99  792  792  ILE ILE B . n 
B 1 100 THR 100 793  793  THR THR B . n 
B 1 101 GLN 101 794  794  GLN GLN B . n 
B 1 102 LEU 102 795  795  LEU LEU B . n 
B 1 103 MET 103 796  796  MET MET B . n 
B 1 104 PRO 104 797  797  PRO PRO B . n 
B 1 105 PHE 105 798  798  PHE PHE B . n 
B 1 106 GLY 106 799  799  GLY GLY B . n 
B 1 107 CYS 107 800  800  CYS CYS B . n 
B 1 108 LEU 108 801  801  LEU LEU B . n 
B 1 109 LEU 109 802  802  LEU LEU B . n 
B 1 110 ASP 110 803  803  ASP ASP B . n 
B 1 111 TYR 111 804  804  TYR TYR B . n 
B 1 112 VAL 112 805  805  VAL VAL B . n 
B 1 113 ARG 113 806  806  ARG ARG B . n 
B 1 114 GLU 114 807  807  GLU GLU B . n 
B 1 115 HIS 115 808  808  HIS HIS B . n 
B 1 116 LYS 116 809  809  LYS LYS B . n 
B 1 117 ASP 117 810  810  ASP ASP B . n 
B 1 118 ASN 118 811  811  ASN ASN B . n 
B 1 119 ILE 119 812  812  ILE ILE B . n 
B 1 120 GLY 120 813  813  GLY GLY B . n 
B 1 121 SER 121 814  814  SER SER B . n 
B 1 122 GLN 122 815  815  GLN GLN B . n 
B 1 123 TYR 123 816  816  TYR TYR B . n 
B 1 124 LEU 124 817  817  LEU LEU B . n 
B 1 125 LEU 125 818  818  LEU LEU B . n 
B 1 126 ASN 126 819  819  ASN ASN B . n 
B 1 127 TRP 127 820  820  TRP TRP B . n 
B 1 128 CYS 128 821  821  CYS CYS B . n 
B 1 129 VAL 129 822  822  VAL VAL B . n 
B 1 130 GLN 130 823  823  GLN GLN B . n 
B 1 131 ILE 131 824  824  ILE ILE B . n 
B 1 132 ALA 132 825  825  ALA ALA B . n 
B 1 133 LYS 133 826  826  LYS LYS B . n 
B 1 134 GLY 134 827  827  GLY GLY B . n 
B 1 135 MET 135 828  828  MET MET B . n 
B 1 136 ASN 136 829  829  ASN ASN B . n 
B 1 137 TYR 137 830  830  TYR TYR B . n 
B 1 138 LEU 138 831  831  LEU LEU B . n 
B 1 139 GLU 139 832  832  GLU GLU B . n 
B 1 140 ASP 140 833  833  ASP ASP B . n 
B 1 141 ARG 141 834  834  ARG ARG B . n 
B 1 142 ARG 142 835  835  ARG ARG B . n 
B 1 143 LEU 143 836  836  LEU LEU B . n 
B 1 144 VAL 144 837  837  VAL VAL B . n 
B 1 145 HIS 145 838  838  HIS HIS B . n 
B 1 146 ARG 146 839  839  ARG ARG B . n 
B 1 147 ASP 147 840  840  ASP ASP B . n 
B 1 148 LEU 148 841  841  LEU LEU B . n 
B 1 149 ALA 149 842  842  ALA ALA B . n 
B 1 150 ALA 150 843  843  ALA ALA B . n 
B 1 151 ARG 151 844  844  ARG ARG B . n 
B 1 152 ASN 152 845  845  ASN ASN B . n 
B 1 153 VAL 153 846  846  VAL VAL B . n 
B 1 154 LEU 154 847  847  LEU LEU B . n 
B 1 155 VAL 155 848  848  VAL VAL B . n 
B 1 156 LYS 156 849  849  LYS LYS B . n 
B 1 157 THR 157 850  850  THR THR B . n 
B 1 158 PRO 158 851  851  PRO PRO B . n 
B 1 159 GLN 159 852  852  GLN GLN B . n 
B 1 160 HIS 160 853  853  HIS HIS B . n 
B 1 161 VAL 161 854  854  VAL VAL B . n 
B 1 162 LYS 162 855  855  LYS LYS B . n 
B 1 163 ILE 163 856  856  ILE ILE B . n 
B 1 164 THR 164 857  857  THR THR B . n 
B 1 165 ASP 165 858  858  ASP ASP B . n 
B 1 166 PHE 166 859  859  PHE PHE B . n 
B 1 167 GLY 167 860  860  GLY GLY B . n 
B 1 168 LEU 168 861  861  LEU LEU B . n 
B 1 169 ALA 169 862  862  ALA ALA B . n 
B 1 170 LYS 170 863  863  LYS LYS B . n 
B 1 171 LEU 171 864  864  LEU LEU B . n 
B 1 172 LEU 172 865  865  LEU LEU B . n 
B 1 173 GLY 173 866  866  GLY GLY B . n 
B 1 174 ALA 174 867  867  ALA ALA B . n 
B 1 175 GLU 175 868  868  GLU GLU B . n 
B 1 176 GLU 176 869  869  GLU GLU B . n 
B 1 177 LYS 177 870  870  LYS LYS B . n 
B 1 178 GLU 178 871  871  GLU GLU B . n 
B 1 179 TYR 179 872  872  TYR TYR B . n 
B 1 180 HIS 180 873  873  HIS HIS B . n 
B 1 181 ALA 181 874  874  ALA ALA B . n 
B 1 182 GLU 182 875  875  GLU GLU B . n 
B 1 183 GLY 183 876  876  GLY GLY B . n 
B 1 184 GLY 184 877  877  GLY GLY B . n 
B 1 185 LYS 185 878  878  LYS LYS B . n 
B 1 186 VAL 186 879  879  VAL VAL B . n 
B 1 187 PRO 187 880  880  PRO PRO B . n 
B 1 188 ILE 188 881  881  ILE ILE B . n 
B 1 189 LYS 189 882  882  LYS LYS B . n 
B 1 190 TRP 190 883  883  TRP TRP B . n 
B 1 191 MET 191 884  884  MET MET B . n 
B 1 192 ALA 192 885  885  ALA ALA B . n 
B 1 193 LEU 193 886  886  LEU LEU B . n 
B 1 194 GLU 194 887  887  GLU GLU B . n 
B 1 195 SER 195 888  888  SER SER B . n 
B 1 196 ILE 196 889  889  ILE ILE B . n 
B 1 197 LEU 197 890  890  LEU LEU B . n 
B 1 198 HIS 198 891  891  HIS HIS B . n 
B 1 199 ARG 199 892  892  ARG ARG B . n 
B 1 200 ILE 200 893  893  ILE ILE B . n 
B 1 201 TYR 201 894  894  TYR TYR B . n 
B 1 202 THR 202 895  895  THR THR B . n 
B 1 203 HIS 203 896  896  HIS HIS B . n 
B 1 204 GLN 204 897  897  GLN GLN B . n 
B 1 205 SER 205 898  898  SER SER B . n 
B 1 206 ASP 206 899  899  ASP ASP B . n 
B 1 207 VAL 207 900  900  VAL VAL B . n 
B 1 208 TRP 208 901  901  TRP TRP B . n 
B 1 209 SER 209 902  902  SER SER B . n 
B 1 210 TYR 210 903  903  TYR TYR B . n 
B 1 211 GLY 211 904  904  GLY GLY B . n 
B 1 212 VAL 212 905  905  VAL VAL B . n 
B 1 213 THR 213 906  906  THR THR B . n 
B 1 214 VAL 214 907  907  VAL VAL B . n 
B 1 215 TRP 215 908  908  TRP TRP B . n 
B 1 216 GLU 216 909  909  GLU GLU B . n 
B 1 217 LEU 217 910  910  LEU LEU B . n 
B 1 218 MET 218 911  911  MET MET B . n 
B 1 219 THR 219 912  912  THR THR B . n 
B 1 220 PHE 220 913  913  PHE PHE B . n 
B 1 221 GLY 221 914  914  GLY GLY B . n 
B 1 222 SER 222 915  915  SER SER B . n 
B 1 223 LYS 223 916  916  LYS LYS B . n 
B 1 224 PRO 224 917  917  PRO PRO B . n 
B 1 225 TYR 225 918  918  TYR TYR B . n 
B 1 226 ASP 226 919  919  ASP ASP B . n 
B 1 227 GLY 227 920  920  GLY GLY B . n 
B 1 228 ILE 228 921  921  ILE ILE B . n 
B 1 229 PRO 229 922  922  PRO PRO B . n 
B 1 230 ALA 230 923  923  ALA ALA B . n 
B 1 231 SER 231 924  924  SER SER B . n 
B 1 232 GLU 232 925  925  GLU GLU B . n 
B 1 233 ILE 233 926  926  ILE ILE B . n 
B 1 234 SER 234 927  927  SER SER B . n 
B 1 235 SER 235 928  928  SER SER B . n 
B 1 236 ILE 236 929  929  ILE ILE B . n 
B 1 237 LEU 237 930  930  LEU LEU B . n 
B 1 238 GLU 238 931  931  GLU GLU B . n 
B 1 239 LYS 239 932  932  LYS LYS B . n 
B 1 240 GLY 240 933  933  GLY GLY B . n 
B 1 241 GLU 241 934  934  GLU GLU B . n 
B 1 242 ARG 242 935  935  ARG ARG B . n 
B 1 243 LEU 243 936  936  LEU LEU B . n 
B 1 244 PRO 244 937  937  PRO PRO B . n 
B 1 245 GLN 245 938  938  GLN GLN B . n 
B 1 246 PRO 246 939  939  PRO PRO B . n 
B 1 247 PRO 247 940  940  PRO PRO B . n 
B 1 248 ILE 248 941  941  ILE ILE B . n 
B 1 249 CYS 249 942  942  CYS CYS B . n 
B 1 250 THR 250 943  943  THR THR B . n 
B 1 251 ILE 251 944  944  ILE ILE B . n 
B 1 252 ASP 252 945  945  ASP ASP B . n 
B 1 253 VAL 253 946  946  VAL VAL B . n 
B 1 254 TYR 254 947  947  TYR TYR B . n 
B 1 255 MET 255 948  948  MET MET B . n 
B 1 256 ILE 256 949  949  ILE ILE B . n 
B 1 257 MET 257 950  950  MET MET B . n 
B 1 258 ARG 258 951  951  ARG ARG B . n 
B 1 259 LYS 259 952  952  LYS LYS B . n 
B 1 260 CYS 260 953  953  CYS CYS B . n 
B 1 261 TRP 261 954  954  TRP TRP B . n 
B 1 262 MET 262 955  955  MET MET B . n 
B 1 263 ILE 263 956  956  ILE ILE B . n 
B 1 264 ASP 264 957  957  ASP ASP B . n 
B 1 265 ALA 265 958  958  ALA ALA B . n 
B 1 266 ASP 266 959  959  ASP ASP B . n 
B 1 267 SER 267 960  960  SER SER B . n 
B 1 268 ARG 268 961  961  ARG ARG B . n 
B 1 269 PRO 269 962  962  PRO PRO B . n 
B 1 270 LYS 270 963  963  LYS LYS B . n 
B 1 271 PHE 271 964  964  PHE PHE B . n 
B 1 272 ARG 272 965  965  ARG ARG B . n 
B 1 273 GLU 273 966  966  GLU GLU B . n 
B 1 274 LEU 274 967  967  LEU LEU B . n 
B 1 275 ILE 275 968  968  ILE ILE B . n 
B 1 276 ILE 276 969  969  ILE ILE B . n 
B 1 277 GLU 277 970  970  GLU GLU B . n 
B 1 278 PHE 278 971  971  PHE PHE B . n 
B 1 279 SER 279 972  972  SER SER B . n 
B 1 280 LYS 280 973  973  LYS LYS B . n 
B 1 281 MET 281 974  974  MET MET B . n 
B 1 282 ALA 282 975  975  ALA ALA B . n 
B 1 283 ARG 283 976  976  ARG ARG B . n 
B 1 284 ASP 284 977  977  ASP ASP B . n 
B 1 285 PRO 285 978  978  PRO PRO B . n 
B 1 286 GLN 286 979  979  GLN GLN B . n 
B 1 287 ARG 287 980  980  ARG ARG B . n 
B 1 288 TYR 288 981  981  TYR TYR B . n 
B 1 289 LEU 289 982  982  LEU LEU B . n 
B 1 290 VAL 290 983  983  VAL VAL B . n 
B 1 291 ILE 291 984  984  ILE ILE B . n 
B 1 292 GLN 292 985  985  GLN GLN B . n 
B 1 293 GLY 293 986  986  GLY GLY B . n 
B 1 294 ASP 294 987  987  ASP ASP B . n 
B 1 295 GLU 295 988  ?    ?   ?   B . n 
B 1 296 ARG 296 989  ?    ?   ?   B . n 
B 1 297 MET 297 990  ?    ?   ?   B . n 
B 1 298 HIS 298 991  ?    ?   ?   B . n 
B 1 299 LEU 299 992  ?    ?   ?   B . n 
B 1 300 PRO 300 993  ?    ?   ?   B . n 
B 1 301 SER 301 994  ?    ?   ?   B . n 
B 1 302 PRO 302 995  ?    ?   ?   B . n 
B 1 303 THR 303 996  ?    ?   ?   B . n 
B 1 304 ASP 304 997  ?    ?   ?   B . n 
B 1 305 SER 305 998  ?    ?   ?   B . n 
B 1 306 ASN 306 999  ?    ?   ?   B . n 
B 1 307 PHE 307 1000 ?    ?   ?   B . n 
B 1 308 TYR 308 1001 ?    ?   ?   B . n 
B 1 309 ARG 309 1002 ?    ?   ?   B . n 
B 1 310 ALA 310 1003 ?    ?   ?   B . n 
B 1 311 LEU 311 1004 ?    ?   ?   B . n 
B 1 312 MET 312 1005 ?    ?   ?   B . n 
B 1 313 ASP 313 1006 ?    ?   ?   B . n 
B 1 314 GLU 314 1007 ?    ?   ?   B . n 
B 1 315 GLU 315 1008 ?    ?   ?   B . n 
B 1 316 ASP 316 1009 ?    ?   ?   B . n 
B 1 317 MET 317 1010 ?    ?   ?   B . n 
B 1 318 ASP 318 1011 ?    ?   ?   B . n 
B 1 319 ASP 319 1012 ?    ?   ?   B . n 
B 1 320 VAL 320 1013 ?    ?   ?   B . n 
B 1 321 VAL 321 1014 ?    ?   ?   B . n 
B 1 322 ASP 322 1015 ?    ?   ?   B . n 
B 1 323 ALA 323 1016 ?    ?   ?   B . n 
B 1 324 ASP 324 1017 ?    ?   ?   B . n 
B 1 325 GLU 325 1018 ?    ?   ?   B . n 
B 1 326 TYR 326 1019 ?    ?   ?   B . n 
B 1 327 LEU 327 1020 ?    ?   ?   B . n 
B 1 328 ILE 328 1021 ?    ?   ?   B . n 
B 1 329 PRO 329 1022 ?    ?   ?   B . n 
B 1 330 GLN 330 1023 ?    ?   ?   B . n 
B 1 331 GLN 331 1024 ?    ?   ?   B . n 
B 1 332 GLY 332 1025 ?    ?   ?   B . n 
C 1 1   GLY 1   694  ?    ?   ?   D . n 
C 1 2   SER 2   695  ?    ?   ?   D . n 
C 1 3   GLY 3   696  ?    ?   ?   D . n 
C 1 4   GLU 4   697  ?    ?   ?   D . n 
C 1 5   ALA 5   698  ?    ?   ?   D . n 
C 1 6   PRO 6   699  ?    ?   ?   D . n 
C 1 7   ASN 7   700  ?    ?   ?   D . n 
C 1 8   GLN 8   701  ?    ?   ?   D . n 
C 1 9   ALA 9   702  ?    ?   ?   D . n 
C 1 10  LEU 10  703  ?    ?   ?   D . n 
C 1 11  LEU 11  704  ?    ?   ?   D . n 
C 1 12  ARG 12  705  ?    ?   ?   D . n 
C 1 13  ILE 13  706  ?    ?   ?   D . n 
C 1 14  LEU 14  707  ?    ?   ?   D . n 
C 1 15  LYS 15  708  ?    ?   ?   D . n 
C 1 16  GLU 16  709  ?    ?   ?   D . n 
C 1 17  THR 17  710  ?    ?   ?   D . n 
C 1 18  GLU 18  711  ?    ?   ?   D . n 
C 1 19  PHE 19  712  ?    ?   ?   D . n 
C 1 20  LYS 20  713  ?    ?   ?   D . n 
C 1 21  LYS 21  714  ?    ?   ?   D . n 
C 1 22  ILE 22  715  ?    ?   ?   D . n 
C 1 23  LYS 23  716  ?    ?   ?   D . n 
C 1 24  VAL 24  717  ?    ?   ?   D . n 
C 1 25  LEU 25  718  ?    ?   ?   D . n 
C 1 26  GLY 26  719  ?    ?   ?   D . n 
C 1 27  SER 27  720  ?    ?   ?   D . n 
C 1 28  GLY 28  721  ?    ?   ?   D . n 
C 1 29  ALA 29  722  ?    ?   ?   D . n 
C 1 30  PHE 30  723  ?    ?   ?   D . n 
C 1 31  GLY 31  724  ?    ?   ?   D . n 
C 1 32  THR 32  725  ?    ?   ?   D . n 
C 1 33  VAL 33  726  ?    ?   ?   D . n 
C 1 34  TYR 34  727  ?    ?   ?   D . n 
C 1 35  LYS 35  728  ?    ?   ?   D . n 
C 1 36  GLY 36  729  ?    ?   ?   D . n 
C 1 37  LEU 37  730  ?    ?   ?   D . n 
C 1 38  TRP 38  731  ?    ?   ?   D . n 
C 1 39  ILE 39  732  ?    ?   ?   D . n 
C 1 40  PRO 40  733  ?    ?   ?   D . n 
C 1 41  GLU 41  734  ?    ?   ?   D . n 
C 1 42  GLY 42  735  ?    ?   ?   D . n 
C 1 43  GLU 43  736  ?    ?   ?   D . n 
C 1 44  LYS 44  737  ?    ?   ?   D . n 
C 1 45  VAL 45  738  ?    ?   ?   D . n 
C 1 46  LYS 46  739  ?    ?   ?   D . n 
C 1 47  ILE 47  740  ?    ?   ?   D . n 
C 1 48  PRO 48  741  ?    ?   ?   D . n 
C 1 49  VAL 49  742  ?    ?   ?   D . n 
C 1 50  ALA 50  743  ?    ?   ?   D . n 
C 1 51  ILE 51  744  ?    ?   ?   D . n 
C 1 52  LYS 52  745  ?    ?   ?   D . n 
C 1 53  GLU 53  746  ?    ?   ?   D . n 
C 1 54  LEU 54  747  ?    ?   ?   D . n 
C 1 55  ARG 55  748  ?    ?   ?   D . n 
C 1 56  GLU 56  749  ?    ?   ?   D . n 
C 1 57  ALA 57  750  ?    ?   ?   D . n 
C 1 58  THR 58  751  ?    ?   ?   D . n 
C 1 59  SER 59  752  ?    ?   ?   D . n 
C 1 60  PRO 60  753  ?    ?   ?   D . n 
C 1 61  LYS 61  754  ?    ?   ?   D . n 
C 1 62  ALA 62  755  ?    ?   ?   D . n 
C 1 63  ASN 63  756  ?    ?   ?   D . n 
C 1 64  LYS 64  757  ?    ?   ?   D . n 
C 1 65  GLU 65  758  ?    ?   ?   D . n 
C 1 66  ILE 66  759  ?    ?   ?   D . n 
C 1 67  LEU 67  760  ?    ?   ?   D . n 
C 1 68  ASP 68  761  ?    ?   ?   D . n 
C 1 69  GLU 69  762  ?    ?   ?   D . n 
C 1 70  ALA 70  763  ?    ?   ?   D . n 
C 1 71  TYR 71  764  ?    ?   ?   D . n 
C 1 72  VAL 72  765  ?    ?   ?   D . n 
C 1 73  MET 73  766  ?    ?   ?   D . n 
C 1 74  ALA 74  767  ?    ?   ?   D . n 
C 1 75  SER 75  768  ?    ?   ?   D . n 
C 1 76  VAL 76  769  ?    ?   ?   D . n 
C 1 77  ASP 77  770  ?    ?   ?   D . n 
C 1 78  ASN 78  771  ?    ?   ?   D . n 
C 1 79  PRO 79  772  ?    ?   ?   D . n 
C 1 80  GLY 80  773  ?    ?   ?   D . n 
C 1 81  ASN 81  774  ?    ?   ?   D . n 
C 1 82  PRO 82  775  ?    ?   ?   D . n 
C 1 83  HIS 83  776  ?    ?   ?   D . n 
C 1 84  VAL 84  777  ?    ?   ?   D . n 
C 1 85  CYS 85  778  ?    ?   ?   D . n 
C 1 86  ARG 86  779  ?    ?   ?   D . n 
C 1 87  LEU 87  780  ?    ?   ?   D . n 
C 1 88  LEU 88  781  ?    ?   ?   D . n 
C 1 89  GLY 89  782  ?    ?   ?   D . n 
C 1 90  ILE 90  783  ?    ?   ?   D . n 
C 1 91  CYS 91  784  ?    ?   ?   D . n 
C 1 92  LEU 92  785  ?    ?   ?   D . n 
C 1 93  THR 93  786  ?    ?   ?   D . n 
C 1 94  SER 94  787  ?    ?   ?   D . n 
C 1 95  THR 95  788  ?    ?   ?   D . n 
C 1 96  VAL 96  789  ?    ?   ?   D . n 
C 1 97  GLN 97  790  ?    ?   ?   D . n 
C 1 98  LEU 98  791  ?    ?   ?   D . n 
C 1 99  ILE 99  792  ?    ?   ?   D . n 
C 1 100 THR 100 793  ?    ?   ?   D . n 
C 1 101 GLN 101 794  ?    ?   ?   D . n 
C 1 102 LEU 102 795  ?    ?   ?   D . n 
C 1 103 MET 103 796  ?    ?   ?   D . n 
C 1 104 PRO 104 797  ?    ?   ?   D . n 
C 1 105 PHE 105 798  ?    ?   ?   D . n 
C 1 106 GLY 106 799  ?    ?   ?   D . n 
C 1 107 CYS 107 800  ?    ?   ?   D . n 
C 1 108 LEU 108 801  ?    ?   ?   D . n 
C 1 109 LEU 109 802  ?    ?   ?   D . n 
C 1 110 ASP 110 803  ?    ?   ?   D . n 
C 1 111 TYR 111 804  ?    ?   ?   D . n 
C 1 112 VAL 112 805  ?    ?   ?   D . n 
C 1 113 ARG 113 806  ?    ?   ?   D . n 
C 1 114 GLU 114 807  ?    ?   ?   D . n 
C 1 115 HIS 115 808  ?    ?   ?   D . n 
C 1 116 LYS 116 809  ?    ?   ?   D . n 
C 1 117 ASP 117 810  ?    ?   ?   D . n 
C 1 118 ASN 118 811  ?    ?   ?   D . n 
C 1 119 ILE 119 812  ?    ?   ?   D . n 
C 1 120 GLY 120 813  ?    ?   ?   D . n 
C 1 121 SER 121 814  ?    ?   ?   D . n 
C 1 122 GLN 122 815  ?    ?   ?   D . n 
C 1 123 TYR 123 816  ?    ?   ?   D . n 
C 1 124 LEU 124 817  ?    ?   ?   D . n 
C 1 125 LEU 125 818  ?    ?   ?   D . n 
C 1 126 ASN 126 819  ?    ?   ?   D . n 
C 1 127 TRP 127 820  ?    ?   ?   D . n 
C 1 128 CYS 128 821  ?    ?   ?   D . n 
C 1 129 VAL 129 822  ?    ?   ?   D . n 
C 1 130 GLN 130 823  ?    ?   ?   D . n 
C 1 131 ILE 131 824  ?    ?   ?   D . n 
C 1 132 ALA 132 825  ?    ?   ?   D . n 
C 1 133 LYS 133 826  ?    ?   ?   D . n 
C 1 134 GLY 134 827  ?    ?   ?   D . n 
C 1 135 MET 135 828  ?    ?   ?   D . n 
C 1 136 ASN 136 829  ?    ?   ?   D . n 
C 1 137 TYR 137 830  ?    ?   ?   D . n 
C 1 138 LEU 138 831  ?    ?   ?   D . n 
C 1 139 GLU 139 832  ?    ?   ?   D . n 
C 1 140 ASP 140 833  ?    ?   ?   D . n 
C 1 141 ARG 141 834  ?    ?   ?   D . n 
C 1 142 ARG 142 835  ?    ?   ?   D . n 
C 1 143 LEU 143 836  ?    ?   ?   D . n 
C 1 144 VAL 144 837  ?    ?   ?   D . n 
C 1 145 HIS 145 838  ?    ?   ?   D . n 
C 1 146 ARG 146 839  ?    ?   ?   D . n 
C 1 147 ASP 147 840  ?    ?   ?   D . n 
C 1 148 LEU 148 841  ?    ?   ?   D . n 
C 1 149 ALA 149 842  ?    ?   ?   D . n 
C 1 150 ALA 150 843  ?    ?   ?   D . n 
C 1 151 ARG 151 844  ?    ?   ?   D . n 
C 1 152 ASN 152 845  ?    ?   ?   D . n 
C 1 153 VAL 153 846  ?    ?   ?   D . n 
C 1 154 LEU 154 847  ?    ?   ?   D . n 
C 1 155 VAL 155 848  ?    ?   ?   D . n 
C 1 156 LYS 156 849  ?    ?   ?   D . n 
C 1 157 THR 157 850  ?    ?   ?   D . n 
C 1 158 PRO 158 851  ?    ?   ?   D . n 
C 1 159 GLN 159 852  ?    ?   ?   D . n 
C 1 160 HIS 160 853  ?    ?   ?   D . n 
C 1 161 VAL 161 854  ?    ?   ?   D . n 
C 1 162 LYS 162 855  ?    ?   ?   D . n 
C 1 163 ILE 163 856  ?    ?   ?   D . n 
C 1 164 THR 164 857  ?    ?   ?   D . n 
C 1 165 ASP 165 858  ?    ?   ?   D . n 
C 1 166 PHE 166 859  ?    ?   ?   D . n 
C 1 167 GLY 167 860  ?    ?   ?   D . n 
C 1 168 LEU 168 861  ?    ?   ?   D . n 
C 1 169 ALA 169 862  ?    ?   ?   D . n 
C 1 170 LYS 170 863  ?    ?   ?   D . n 
C 1 171 LEU 171 864  ?    ?   ?   D . n 
C 1 172 LEU 172 865  ?    ?   ?   D . n 
C 1 173 GLY 173 866  ?    ?   ?   D . n 
C 1 174 ALA 174 867  ?    ?   ?   D . n 
C 1 175 GLU 175 868  ?    ?   ?   D . n 
C 1 176 GLU 176 869  ?    ?   ?   D . n 
C 1 177 LYS 177 870  ?    ?   ?   D . n 
C 1 178 GLU 178 871  ?    ?   ?   D . n 
C 1 179 TYR 179 872  ?    ?   ?   D . n 
C 1 180 HIS 180 873  ?    ?   ?   D . n 
C 1 181 ALA 181 874  ?    ?   ?   D . n 
C 1 182 GLU 182 875  ?    ?   ?   D . n 
C 1 183 GLY 183 876  ?    ?   ?   D . n 
C 1 184 GLY 184 877  ?    ?   ?   D . n 
C 1 185 LYS 185 878  ?    ?   ?   D . n 
C 1 186 VAL 186 879  ?    ?   ?   D . n 
C 1 187 PRO 187 880  ?    ?   ?   D . n 
C 1 188 ILE 188 881  ?    ?   ?   D . n 
C 1 189 LYS 189 882  ?    ?   ?   D . n 
C 1 190 TRP 190 883  ?    ?   ?   D . n 
C 1 191 MET 191 884  ?    ?   ?   D . n 
C 1 192 ALA 192 885  ?    ?   ?   D . n 
C 1 193 LEU 193 886  ?    ?   ?   D . n 
C 1 194 GLU 194 887  ?    ?   ?   D . n 
C 1 195 SER 195 888  ?    ?   ?   D . n 
C 1 196 ILE 196 889  ?    ?   ?   D . n 
C 1 197 LEU 197 890  ?    ?   ?   D . n 
C 1 198 HIS 198 891  ?    ?   ?   D . n 
C 1 199 ARG 199 892  ?    ?   ?   D . n 
C 1 200 ILE 200 893  ?    ?   ?   D . n 
C 1 201 TYR 201 894  ?    ?   ?   D . n 
C 1 202 THR 202 895  ?    ?   ?   D . n 
C 1 203 HIS 203 896  ?    ?   ?   D . n 
C 1 204 GLN 204 897  ?    ?   ?   D . n 
C 1 205 SER 205 898  ?    ?   ?   D . n 
C 1 206 ASP 206 899  ?    ?   ?   D . n 
C 1 207 VAL 207 900  ?    ?   ?   D . n 
C 1 208 TRP 208 901  ?    ?   ?   D . n 
C 1 209 SER 209 902  ?    ?   ?   D . n 
C 1 210 TYR 210 903  ?    ?   ?   D . n 
C 1 211 GLY 211 904  ?    ?   ?   D . n 
C 1 212 VAL 212 905  ?    ?   ?   D . n 
C 1 213 THR 213 906  ?    ?   ?   D . n 
C 1 214 VAL 214 907  ?    ?   ?   D . n 
C 1 215 TRP 215 908  ?    ?   ?   D . n 
C 1 216 GLU 216 909  ?    ?   ?   D . n 
C 1 217 LEU 217 910  ?    ?   ?   D . n 
C 1 218 MET 218 911  ?    ?   ?   D . n 
C 1 219 THR 219 912  ?    ?   ?   D . n 
C 1 220 PHE 220 913  ?    ?   ?   D . n 
C 1 221 GLY 221 914  ?    ?   ?   D . n 
C 1 222 SER 222 915  ?    ?   ?   D . n 
C 1 223 LYS 223 916  ?    ?   ?   D . n 
C 1 224 PRO 224 917  ?    ?   ?   D . n 
C 1 225 TYR 225 918  ?    ?   ?   D . n 
C 1 226 ASP 226 919  ?    ?   ?   D . n 
C 1 227 GLY 227 920  ?    ?   ?   D . n 
C 1 228 ILE 228 921  ?    ?   ?   D . n 
C 1 229 PRO 229 922  ?    ?   ?   D . n 
C 1 230 ALA 230 923  ?    ?   ?   D . n 
C 1 231 SER 231 924  ?    ?   ?   D . n 
C 1 232 GLU 232 925  ?    ?   ?   D . n 
C 1 233 ILE 233 926  ?    ?   ?   D . n 
C 1 234 SER 234 927  ?    ?   ?   D . n 
C 1 235 SER 235 928  ?    ?   ?   D . n 
C 1 236 ILE 236 929  ?    ?   ?   D . n 
C 1 237 LEU 237 930  ?    ?   ?   D . n 
C 1 238 GLU 238 931  ?    ?   ?   D . n 
C 1 239 LYS 239 932  ?    ?   ?   D . n 
C 1 240 GLY 240 933  ?    ?   ?   D . n 
C 1 241 GLU 241 934  ?    ?   ?   D . n 
C 1 242 ARG 242 935  ?    ?   ?   D . n 
C 1 243 LEU 243 936  ?    ?   ?   D . n 
C 1 244 PRO 244 937  ?    ?   ?   D . n 
C 1 245 GLN 245 938  ?    ?   ?   D . n 
C 1 246 PRO 246 939  ?    ?   ?   D . n 
C 1 247 PRO 247 940  ?    ?   ?   D . n 
C 1 248 ILE 248 941  ?    ?   ?   D . n 
C 1 249 CYS 249 942  ?    ?   ?   D . n 
C 1 250 THR 250 943  ?    ?   ?   D . n 
C 1 251 ILE 251 944  ?    ?   ?   D . n 
C 1 252 ASP 252 945  ?    ?   ?   D . n 
C 1 253 VAL 253 946  ?    ?   ?   D . n 
C 1 254 TYR 254 947  ?    ?   ?   D . n 
C 1 255 MET 255 948  ?    ?   ?   D . n 
C 1 256 ILE 256 949  ?    ?   ?   D . n 
C 1 257 MET 257 950  ?    ?   ?   D . n 
C 1 258 ARG 258 951  ?    ?   ?   D . n 
C 1 259 LYS 259 952  ?    ?   ?   D . n 
C 1 260 CYS 260 953  ?    ?   ?   D . n 
C 1 261 TRP 261 954  ?    ?   ?   D . n 
C 1 262 MET 262 955  ?    ?   ?   D . n 
C 1 263 ILE 263 956  ?    ?   ?   D . n 
C 1 264 ASP 264 957  ?    ?   ?   D . n 
C 1 265 ALA 265 958  ?    ?   ?   D . n 
C 1 266 ASP 266 959  ?    ?   ?   D . n 
C 1 267 SER 267 960  ?    ?   ?   D . n 
C 1 268 ARG 268 961  ?    ?   ?   D . n 
C 1 269 PRO 269 962  ?    ?   ?   D . n 
C 1 270 LYS 270 963  ?    ?   ?   D . n 
C 1 271 PHE 271 964  ?    ?   ?   D . n 
C 1 272 ARG 272 965  ?    ?   ?   D . n 
C 1 273 GLU 273 966  ?    ?   ?   D . n 
C 1 274 LEU 274 967  ?    ?   ?   D . n 
C 1 275 ILE 275 968  ?    ?   ?   D . n 
C 1 276 ILE 276 969  ?    ?   ?   D . n 
C 1 277 GLU 277 970  ?    ?   ?   D . n 
C 1 278 PHE 278 971  ?    ?   ?   D . n 
C 1 279 SER 279 972  ?    ?   ?   D . n 
C 1 280 LYS 280 973  ?    ?   ?   D . n 
C 1 281 MET 281 974  ?    ?   ?   D . n 
C 1 282 ALA 282 975  ?    ?   ?   D . n 
C 1 283 ARG 283 976  ?    ?   ?   D . n 
C 1 284 ASP 284 977  ?    ?   ?   D . n 
C 1 285 PRO 285 978  ?    ?   ?   D . n 
C 1 286 GLN 286 979  ?    ?   ?   D . n 
C 1 287 ARG 287 980  ?    ?   ?   D . n 
C 1 288 TYR 288 981  ?    ?   ?   D . n 
C 1 289 LEU 289 982  ?    ?   ?   D . n 
C 1 290 VAL 290 983  ?    ?   ?   D . n 
C 1 291 ILE 291 984  ?    ?   ?   D . n 
C 1 292 GLN 292 985  ?    ?   ?   D . n 
C 1 293 GLY 293 986  ?    ?   ?   D . n 
C 1 294 ASP 294 987  ?    ?   ?   D . n 
C 1 295 GLU 295 988  ?    ?   ?   D . n 
C 1 296 ARG 296 989  ?    ?   ?   D . n 
C 1 297 MET 297 990  ?    ?   ?   D . n 
C 1 298 HIS 298 991  ?    ?   ?   D . n 
C 1 299 LEU 299 992  ?    ?   ?   D . n 
C 1 300 PRO 300 993  ?    ?   ?   D . n 
C 1 301 SER 301 994  ?    ?   ?   D . n 
C 1 302 PRO 302 995  ?    ?   ?   D . n 
C 1 303 THR 303 996  ?    ?   ?   D . n 
C 1 304 ASP 304 997  ?    ?   ?   D . n 
C 1 305 SER 305 998  ?    ?   ?   D . n 
C 1 306 ASN 306 999  ?    ?   ?   D . n 
C 1 307 PHE 307 1000 ?    ?   ?   D . n 
C 1 308 TYR 308 1001 ?    ?   ?   D . n 
C 1 309 ARG 309 1002 ?    ?   ?   D . n 
C 1 310 ALA 310 1003 ?    ?   ?   D . n 
C 1 311 LEU 311 1004 ?    ?   ?   D . n 
C 1 312 MET 312 1005 1005 MET MET D . n 
C 1 313 ASP 313 1006 1006 ASP ASP D . n 
C 1 314 GLU 314 1007 1007 GLU GLU D . n 
C 1 315 GLU 315 1008 1008 GLU GLU D . n 
C 1 316 ASP 316 1009 1009 ASP ASP D . n 
C 1 317 MET 317 1010 1010 MET MET D . n 
C 1 318 ASP 318 1011 1011 ASP ASP D . n 
C 1 319 ASP 319 1012 1012 ASP ASP D . n 
C 1 320 VAL 320 1013 1013 VAL VAL D . n 
C 1 321 VAL 321 1014 1014 VAL VAL D . n 
C 1 322 ASP 322 1015 1015 ASP ASP D . n 
C 1 323 ALA 323 1016 1016 ALA ALA D . n 
C 1 324 ASP 324 1017 1017 ASP ASP D . n 
C 1 325 GLU 325 1018 1018 GLU GLU D . n 
C 1 326 TYR 326 1019 1019 TYR TYR D . n 
C 1 327 LEU 327 1020 1020 LEU LEU D . n 
C 1 328 ILE 328 1021 1021 ILE ILE D . n 
C 1 329 PRO 329 1022 ?    ?   ?   D . n 
C 1 330 GLN 330 1023 ?    ?   ?   D . n 
C 1 331 GLN 331 1024 ?    ?   ?   D . n 
C 1 332 GLY 332 1025 ?    ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IZ7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IZ7 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 A1IZ7 1   1101 1001 A1IZ7 INH A . 
E 2 A1IZ7 1   1101 1001 A1IZ7 INH B . 
F 3 HOH   1   1201 109  HOH   HOH A . 
F 3 HOH   2   1202 29   HOH   HOH A . 
F 3 HOH   3   1203 216  HOH   HOH A . 
F 3 HOH   4   1204 183  HOH   HOH A . 
F 3 HOH   5   1205 231  HOH   HOH A . 
F 3 HOH   6   1206 24   HOH   HOH A . 
F 3 HOH   7   1207 125  HOH   HOH A . 
F 3 HOH   8   1208 57   HOH   HOH A . 
F 3 HOH   9   1209 6    HOH   HOH A . 
F 3 HOH   10  1210 10   HOH   HOH A . 
F 3 HOH   11  1211 66   HOH   HOH A . 
F 3 HOH   12  1212 3    HOH   HOH A . 
F 3 HOH   13  1213 43   HOH   HOH A . 
F 3 HOH   14  1214 65   HOH   HOH A . 
F 3 HOH   15  1215 92   HOH   HOH A . 
F 3 HOH   16  1216 190  HOH   HOH A . 
F 3 HOH   17  1217 174  HOH   HOH A . 
F 3 HOH   18  1218 162  HOH   HOH A . 
F 3 HOH   19  1219 19   HOH   HOH A . 
F 3 HOH   20  1220 184  HOH   HOH A . 
F 3 HOH   21  1221 36   HOH   HOH A . 
F 3 HOH   22  1222 95   HOH   HOH A . 
F 3 HOH   23  1223 14   HOH   HOH A . 
F 3 HOH   24  1224 167  HOH   HOH A . 
F 3 HOH   25  1225 96   HOH   HOH A . 
F 3 HOH   26  1226 4    HOH   HOH A . 
F 3 HOH   27  1227 193  HOH   HOH A . 
F 3 HOH   28  1228 16   HOH   HOH A . 
F 3 HOH   29  1229 100  HOH   HOH A . 
F 3 HOH   30  1230 119  HOH   HOH A . 
F 3 HOH   31  1231 35   HOH   HOH A . 
F 3 HOH   32  1232 232  HOH   HOH A . 
F 3 HOH   33  1233 116  HOH   HOH A . 
F 3 HOH   34  1234 103  HOH   HOH A . 
F 3 HOH   35  1235 198  HOH   HOH A . 
F 3 HOH   36  1236 112  HOH   HOH A . 
F 3 HOH   37  1237 163  HOH   HOH A . 
F 3 HOH   38  1238 229  HOH   HOH A . 
F 3 HOH   39  1239 177  HOH   HOH A . 
F 3 HOH   40  1240 168  HOH   HOH A . 
F 3 HOH   41  1241 74   HOH   HOH A . 
F 3 HOH   42  1242 200  HOH   HOH A . 
F 3 HOH   43  1243 77   HOH   HOH A . 
F 3 HOH   44  1244 89   HOH   HOH A . 
F 3 HOH   45  1245 55   HOH   HOH A . 
F 3 HOH   46  1246 227  HOH   HOH A . 
F 3 HOH   47  1247 40   HOH   HOH A . 
F 3 HOH   48  1248 48   HOH   HOH A . 
F 3 HOH   49  1249 185  HOH   HOH A . 
F 3 HOH   50  1250 45   HOH   HOH A . 
F 3 HOH   51  1251 159  HOH   HOH A . 
F 3 HOH   52  1252 123  HOH   HOH A . 
F 3 HOH   53  1253 32   HOH   HOH A . 
F 3 HOH   54  1254 122  HOH   HOH A . 
F 3 HOH   55  1255 30   HOH   HOH A . 
F 3 HOH   56  1256 169  HOH   HOH A . 
F 3 HOH   57  1257 75   HOH   HOH A . 
F 3 HOH   58  1258 67   HOH   HOH A . 
F 3 HOH   59  1259 207  HOH   HOH A . 
F 3 HOH   60  1260 72   HOH   HOH A . 
F 3 HOH   61  1261 64   HOH   HOH A . 
F 3 HOH   62  1262 234  HOH   HOH A . 
F 3 HOH   63  1263 8    HOH   HOH A . 
F 3 HOH   64  1264 38   HOH   HOH A . 
F 3 HOH   65  1265 15   HOH   HOH A . 
F 3 HOH   66  1266 47   HOH   HOH A . 
F 3 HOH   67  1267 51   HOH   HOH A . 
F 3 HOH   68  1268 114  HOH   HOH A . 
F 3 HOH   69  1269 113  HOH   HOH A . 
F 3 HOH   70  1270 178  HOH   HOH A . 
F 3 HOH   71  1271 191  HOH   HOH A . 
F 3 HOH   72  1272 212  HOH   HOH A . 
F 3 HOH   73  1273 164  HOH   HOH A . 
F 3 HOH   74  1274 84   HOH   HOH A . 
F 3 HOH   75  1275 27   HOH   HOH A . 
F 3 HOH   76  1276 60   HOH   HOH A . 
F 3 HOH   77  1277 130  HOH   HOH A . 
F 3 HOH   78  1278 9    HOH   HOH A . 
F 3 HOH   79  1279 73   HOH   HOH A . 
F 3 HOH   80  1280 153  HOH   HOH A . 
F 3 HOH   81  1281 80   HOH   HOH A . 
F 3 HOH   82  1282 56   HOH   HOH A . 
F 3 HOH   83  1283 126  HOH   HOH A . 
F 3 HOH   84  1284 139  HOH   HOH A . 
F 3 HOH   85  1285 25   HOH   HOH A . 
F 3 HOH   86  1286 144  HOH   HOH A . 
F 3 HOH   87  1287 17   HOH   HOH A . 
F 3 HOH   88  1288 131  HOH   HOH A . 
F 3 HOH   89  1289 129  HOH   HOH A . 
F 3 HOH   90  1290 233  HOH   HOH A . 
F 3 HOH   91  1291 53   HOH   HOH A . 
F 3 HOH   92  1292 26   HOH   HOH A . 
F 3 HOH   93  1293 91   HOH   HOH A . 
F 3 HOH   94  1294 34   HOH   HOH A . 
F 3 HOH   95  1295 176  HOH   HOH A . 
F 3 HOH   96  1296 1    HOH   HOH A . 
F 3 HOH   97  1297 219  HOH   HOH A . 
F 3 HOH   98  1298 128  HOH   HOH A . 
F 3 HOH   99  1299 237  HOH   HOH A . 
F 3 HOH   100 1300 142  HOH   HOH A . 
F 3 HOH   101 1301 226  HOH   HOH A . 
F 3 HOH   102 1302 81   HOH   HOH A . 
F 3 HOH   103 1303 215  HOH   HOH A . 
F 3 HOH   104 1304 115  HOH   HOH A . 
F 3 HOH   105 1305 239  HOH   HOH A . 
G 3 HOH   1   1201 208  HOH   HOH B . 
G 3 HOH   2   1202 245  HOH   HOH B . 
G 3 HOH   3   1203 160  HOH   HOH B . 
G 3 HOH   4   1204 242  HOH   HOH B . 
G 3 HOH   5   1205 202  HOH   HOH B . 
G 3 HOH   6   1206 106  HOH   HOH B . 
G 3 HOH   7   1207 107  HOH   HOH B . 
G 3 HOH   8   1208 199  HOH   HOH B . 
G 3 HOH   9   1209 46   HOH   HOH B . 
G 3 HOH   10  1210 13   HOH   HOH B . 
G 3 HOH   11  1211 49   HOH   HOH B . 
G 3 HOH   12  1212 121  HOH   HOH B . 
G 3 HOH   13  1213 220  HOH   HOH B . 
G 3 HOH   14  1214 217  HOH   HOH B . 
G 3 HOH   15  1215 7    HOH   HOH B . 
G 3 HOH   16  1216 97   HOH   HOH B . 
G 3 HOH   17  1217 201  HOH   HOH B . 
G 3 HOH   18  1218 88   HOH   HOH B . 
G 3 HOH   19  1219 39   HOH   HOH B . 
G 3 HOH   20  1220 79   HOH   HOH B . 
G 3 HOH   21  1221 127  HOH   HOH B . 
G 3 HOH   22  1222 21   HOH   HOH B . 
G 3 HOH   23  1223 31   HOH   HOH B . 
G 3 HOH   24  1224 41   HOH   HOH B . 
G 3 HOH   25  1225 197  HOH   HOH B . 
G 3 HOH   26  1226 155  HOH   HOH B . 
G 3 HOH   27  1227 70   HOH   HOH B . 
G 3 HOH   28  1228 214  HOH   HOH B . 
G 3 HOH   29  1229 37   HOH   HOH B . 
G 3 HOH   30  1230 172  HOH   HOH B . 
G 3 HOH   31  1231 52   HOH   HOH B . 
G 3 HOH   32  1232 137  HOH   HOH B . 
G 3 HOH   33  1233 141  HOH   HOH B . 
G 3 HOH   34  1234 173  HOH   HOH B . 
G 3 HOH   35  1235 54   HOH   HOH B . 
G 3 HOH   36  1236 111  HOH   HOH B . 
G 3 HOH   37  1237 69   HOH   HOH B . 
G 3 HOH   38  1238 58   HOH   HOH B . 
G 3 HOH   39  1239 71   HOH   HOH B . 
G 3 HOH   40  1240 12   HOH   HOH B . 
G 3 HOH   41  1241 23   HOH   HOH B . 
G 3 HOH   42  1242 18   HOH   HOH B . 
G 3 HOH   43  1243 145  HOH   HOH B . 
G 3 HOH   44  1244 50   HOH   HOH B . 
G 3 HOH   45  1245 85   HOH   HOH B . 
G 3 HOH   46  1246 194  HOH   HOH B . 
G 3 HOH   47  1247 161  HOH   HOH B . 
G 3 HOH   48  1248 33   HOH   HOH B . 
G 3 HOH   49  1249 118  HOH   HOH B . 
G 3 HOH   50  1250 228  HOH   HOH B . 
G 3 HOH   51  1251 223  HOH   HOH B . 
G 3 HOH   52  1252 204  HOH   HOH B . 
G 3 HOH   53  1253 187  HOH   HOH B . 
G 3 HOH   54  1254 63   HOH   HOH B . 
G 3 HOH   55  1255 175  HOH   HOH B . 
G 3 HOH   56  1256 87   HOH   HOH B . 
G 3 HOH   57  1257 225  HOH   HOH B . 
G 3 HOH   58  1258 110  HOH   HOH B . 
G 3 HOH   59  1259 98   HOH   HOH B . 
G 3 HOH   60  1260 62   HOH   HOH B . 
G 3 HOH   61  1261 117  HOH   HOH B . 
G 3 HOH   62  1262 86   HOH   HOH B . 
G 3 HOH   63  1263 170  HOH   HOH B . 
G 3 HOH   64  1264 236  HOH   HOH B . 
G 3 HOH   65  1265 22   HOH   HOH B . 
G 3 HOH   66  1266 11   HOH   HOH B . 
G 3 HOH   67  1267 42   HOH   HOH B . 
G 3 HOH   68  1268 189  HOH   HOH B . 
G 3 HOH   69  1269 108  HOH   HOH B . 
G 3 HOH   70  1270 90   HOH   HOH B . 
G 3 HOH   71  1271 132  HOH   HOH B . 
G 3 HOH   72  1272 209  HOH   HOH B . 
G 3 HOH   73  1273 99   HOH   HOH B . 
G 3 HOH   74  1274 166  HOH   HOH B . 
G 3 HOH   75  1275 205  HOH   HOH B . 
G 3 HOH   76  1276 179  HOH   HOH B . 
G 3 HOH   77  1277 59   HOH   HOH B . 
G 3 HOH   78  1278 218  HOH   HOH B . 
G 3 HOH   79  1279 156  HOH   HOH B . 
G 3 HOH   80  1280 224  HOH   HOH B . 
G 3 HOH   81  1281 206  HOH   HOH B . 
G 3 HOH   82  1282 158  HOH   HOH B . 
G 3 HOH   83  1283 133  HOH   HOH B . 
G 3 HOH   84  1284 196  HOH   HOH B . 
G 3 HOH   85  1285 135  HOH   HOH B . 
H 3 HOH   1   1101 76   HOH   HOH D . 
H 3 HOH   2   1102 5    HOH   HOH D . 
H 3 HOH   3   1103 105  HOH   HOH D . 
H 3 HOH   4   1104 83   HOH   HOH D . 
H 3 HOH   5   1105 143  HOH   HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .                      1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                      2 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.11.8 (26-JUL-2023)' 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   121.29 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GC4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     134.524 
_cell.length_a_esd                 ? 
_cell.length_b                     84.246 
_cell.length_b_esd                 ? 
_cell.length_c                     96.465 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GC4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GC4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.32 
_exptl_crystal.description                  'plate like' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'alcohols 10%, MB1 0.1M pH 6.5, EDO_P8K 30%w/v (morpheus screen D2)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-10-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GC4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.415 
_reflns.d_resolution_low                               65.850 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     23451 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           78.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.415 
_reflns_shell.d_res_low                                     2.633 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1173 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.655 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.33770 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.44140 
_refine.aniso_B[2][2]                            0.14020 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -0.47790 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               53.45 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.921 
_refine.correlation_coeff_Fo_to_Fc_free          0.897 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GC4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.415 
_refine.ls_d_res_low                             26.91 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     23425 
_refine.ls_number_reflns_R_free                  1139 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    66.2 
_refine.ls_percent_reflns_R_free                 4.860 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2180 
_refine.ls_R_factor_R_free                       0.2481 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2165 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.315 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.309 
_refine.pdbx_overall_SU_R_Blow_DPI               0.685 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.704 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        9GC4 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.36 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.415 
_refine_hist.d_res_low                        26.91 
_refine_hist.number_atoms_solvent             195 
_refine_hist.number_atoms_total               4963 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4702 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         66 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 4880 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.91  ? 6602 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1735 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 798  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4880 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 2.81  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 19.95 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 622  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 3876 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.42 
_refine_ls_shell.d_res_low                        2.55 
_refine_ls_shell.number_reflns_all                469 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             451 
_refine_ls_shell.percent_reflns_obs               8.81 
_refine_ls_shell.percent_reflns_R_free            3.84 
_refine_ls_shell.R_factor_all                     0.2819 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2832 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2483 
# 
_struct.entry_id                     9GC4 
_struct.title                        'Highly optimized CNS penetrant inhibitors of EGFR Exon20 Insertion Mutations' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9GC4 
_struct_keywords.text            'EGFR, Exon20, NPG, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    EGFR_HUMAN 
_struct_ref.pdbx_db_accession          P00533 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHV
CRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKIT
DFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLP
QPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDAD
EYLIPQQG
;
_struct_ref.pdbx_align_begin           695 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GC4 A 2 ? 332 ? P00533 695 ? 1022 ? 695 1025 
2 1 9GC4 B 2 ? 332 ? P00533 695 ? 1022 ? 695 1025 
3 1 9GC4 D 2 ? 332 ? P00533 695 ? 1022 ? 695 1025 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GC4 GLY A 1   ? UNP P00533 ?   ?   'expression tag'      694 1  
1 9GC4 ASN A 78  ? UNP P00533 ?   ?   insertion             771 2  
1 9GC4 PRO A 79  ? UNP P00533 ?   ?   insertion             772 3  
1 9GC4 GLY A 80  ? UNP P00533 ?   ?   insertion             773 4  
1 9GC4 ARG A 258 ? UNP P00533 VAL 948 'engineered mutation' 951 5  
2 9GC4 GLY B 1   ? UNP P00533 ?   ?   'expression tag'      694 6  
2 9GC4 ASN B 78  ? UNP P00533 ?   ?   insertion             771 7  
2 9GC4 PRO B 79  ? UNP P00533 ?   ?   insertion             772 8  
2 9GC4 GLY B 80  ? UNP P00533 ?   ?   insertion             773 9  
2 9GC4 ARG B 258 ? UNP P00533 VAL 948 'engineered mutation' 951 10 
3 9GC4 GLY D 1   ? UNP P00533 ?   ?   'expression tag'      694 11 
3 9GC4 ASN D 78  ? UNP P00533 ?   ?   insertion             771 12 
3 9GC4 PRO D 79  ? UNP P00533 ?   ?   insertion             772 13 
3 9GC4 GLY D 80  ? UNP P00533 ?   ?   insertion             773 14 
3 9GC4 ARG D 258 ? UNP P00533 VAL 948 'engineered mutation' 951 15 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA dimeric   2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  13670 ? 
2 'ABSA (A^2)' 1440  ? 
2 MORE         -3    ? 
2 'SSA (A^2)'  14430 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,F     
2 1 B,C,E,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 15  ? THR A 17  ? LYS A 708 THR A 710 5 ? 3  
HELX_P HELX_P2  AA2 ALA A 62  ? SER A 75  ? ALA A 755 SER A 768 1 ? 14 
HELX_P HELX_P3  AA3 VAL A 76  ? ASN A 78  ? VAL A 769 ASN A 771 5 ? 3  
HELX_P HELX_P4  AA4 CYS A 107 ? HIS A 115 ? CYS A 800 HIS A 808 1 ? 9  
HELX_P HELX_P5  AA5 GLY A 120 ? ARG A 141 ? GLY A 813 ARG A 834 1 ? 22 
HELX_P HELX_P6  AA6 ALA A 149 ? ARG A 151 ? ALA A 842 ARG A 844 5 ? 3  
HELX_P HELX_P7  AA7 GLY A 167 ? LEU A 172 ? GLY A 860 LEU A 865 1 ? 6  
HELX_P HELX_P8  AA8 PRO A 187 ? MET A 191 ? PRO A 880 MET A 884 5 ? 5  
HELX_P HELX_P9  AA9 ALA A 192 ? ARG A 199 ? ALA A 885 ARG A 892 1 ? 8  
HELX_P HELX_P10 AB1 THR A 202 ? THR A 219 ? THR A 895 THR A 912 1 ? 18 
HELX_P HELX_P11 AB2 PRO A 229 ? SER A 231 ? PRO A 922 SER A 924 5 ? 3  
HELX_P HELX_P12 AB3 GLU A 232 ? LYS A 239 ? GLU A 925 LYS A 932 1 ? 8  
HELX_P HELX_P13 AB4 THR A 250 ? TRP A 261 ? THR A 943 TRP A 954 1 ? 12 
HELX_P HELX_P14 AB5 ASP A 264 ? ARG A 268 ? ASP A 957 ARG A 961 5 ? 5  
HELX_P HELX_P15 AB6 LYS A 270 ? ALA A 282 ? LYS A 963 ALA A 975 1 ? 13 
HELX_P HELX_P16 AB7 ASP A 284 ? LEU A 289 ? ASP A 977 LEU A 982 1 ? 6  
HELX_P HELX_P17 AB8 LYS B 15  ? THR B 17  ? LYS B 708 THR B 710 5 ? 3  
HELX_P HELX_P18 AB9 ALA B 62  ? VAL B 76  ? ALA B 755 VAL B 769 1 ? 15 
HELX_P HELX_P19 AC1 CYS B 107 ? HIS B 115 ? CYS B 800 HIS B 808 1 ? 9  
HELX_P HELX_P20 AC2 LYS B 116 ? ILE B 119 ? LYS B 809 ILE B 812 5 ? 4  
HELX_P HELX_P21 AC3 GLY B 120 ? ARG B 141 ? GLY B 813 ARG B 834 1 ? 22 
HELX_P HELX_P22 AC4 ALA B 149 ? ARG B 151 ? ALA B 842 ARG B 844 5 ? 3  
HELX_P HELX_P23 AC5 GLY B 167 ? LEU B 172 ? GLY B 860 LEU B 865 1 ? 6  
HELX_P HELX_P24 AC6 PRO B 187 ? MET B 191 ? PRO B 880 MET B 884 5 ? 5  
HELX_P HELX_P25 AC7 ALA B 192 ? ARG B 199 ? ALA B 885 ARG B 892 1 ? 8  
HELX_P HELX_P26 AC8 THR B 202 ? THR B 219 ? THR B 895 THR B 912 1 ? 18 
HELX_P HELX_P27 AC9 PRO B 229 ? SER B 231 ? PRO B 922 SER B 924 5 ? 3  
HELX_P HELX_P28 AD1 GLU B 232 ? LYS B 239 ? GLU B 925 LYS B 932 1 ? 8  
HELX_P HELX_P29 AD2 THR B 250 ? TRP B 261 ? THR B 943 TRP B 954 1 ? 12 
HELX_P HELX_P30 AD3 ASP B 264 ? ARG B 268 ? ASP B 957 ARG B 961 5 ? 5  
HELX_P HELX_P31 AD4 LYS B 270 ? ALA B 282 ? LYS B 963 ALA B 975 1 ? 13 
HELX_P HELX_P32 AD5 ASP B 284 ? LEU B 289 ? ASP B 977 LEU B 982 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A CYS 107 SG ? ? ? 1_555 D A1IZ7 . C22 ? ? A CYS 800 A A1IZ7 1101 1_555 ? ? ? ? ? ? ? 1.811 ? ? 
covale2 covale none ? B CYS 107 SG ? ? ? 1_555 E A1IZ7 . C22 ? ? B CYS 800 B A1IZ7 1101 1_555 ? ? ? ? ? ? ? 1.797 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1IZ7 D . ? CYS A 107 ? A1IZ7 A 1101 ? 1_555 CYS A 800 ? 1_555 C22 SG CYS 1 A1IZ7 None 'Covalent chemical modification' 
2 A1IZ7 E . ? CYS B 107 ? A1IZ7 B 1101 ? 1_555 CYS B 800 ? 1_555 C22 SG CYS 1 A1IZ7 None 'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASN 78 A . ? ASN 771 A PRO 79 A ? PRO 772 A 1 4.76 
2 ASN 78 B . ? ASN 771 B PRO 79 B ? PRO 772 B 1 4.23 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 12  ? ILE A 13  ? ARG A 705 ILE A 706 
AA1 2 GLY A 89  ? LEU A 92  ? GLY A 782 LEU A 785 
AA1 3 VAL A 96  ? GLN A 101 ? VAL A 789 GLN A 794 
AA1 4 ILE A 47  ? LEU A 54  ? ILE A 740 LEU A 747 
AA1 5 GLY A 31  ? TRP A 38  ? GLY A 724 TRP A 731 
AA1 6 PHE A 19  ? SER A 27  ? PHE A 712 SER A 720 
AA2 1 VAL A 153 ? THR A 157 ? VAL A 846 THR A 850 
AA2 2 HIS A 160 ? ILE A 163 ? HIS A 853 ILE A 856 
AA3 1 ARG B 12  ? ILE B 13  ? ARG B 705 ILE B 706 
AA3 2 GLY B 89  ? LEU B 92  ? GLY B 782 LEU B 785 
AA3 3 VAL B 96  ? GLN B 101 ? VAL B 789 GLN B 794 
AA3 4 ILE B 47  ? LEU B 54  ? ILE B 740 LEU B 747 
AA3 5 GLY B 31  ? TRP B 38  ? GLY B 724 TRP B 731 
AA3 6 PHE B 19  ? SER B 27  ? PHE B 712 SER B 720 
AA4 1 VAL B 153 ? THR B 157 ? VAL B 846 THR B 850 
AA4 2 HIS B 160 ? ILE B 163 ? HIS B 853 ILE B 856 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 12  ? N ARG A 705 O ILE A 90  ? O ILE A 783 
AA1 2 3 N GLY A 89  ? N GLY A 782 O ILE A 99  ? O ILE A 792 
AA1 3 4 O LEU A 98  ? O LEU A 791 N LYS A 52  ? N LYS A 745 
AA1 4 5 O GLU A 53  ? O GLU A 746 N THR A 32  ? N THR A 725 
AA1 5 6 O VAL A 33  ? O VAL A 726 N GLY A 26  ? N GLY A 719 
AA2 1 2 N LEU A 154 ? N LEU A 847 O LYS A 162 ? O LYS A 855 
AA3 1 2 N ARG B 12  ? N ARG B 705 O ILE B 90  ? O ILE B 783 
AA3 2 3 N GLY B 89  ? N GLY B 782 O ILE B 99  ? O ILE B 792 
AA3 3 4 O LEU B 98  ? O LEU B 791 N LYS B 52  ? N LYS B 745 
AA3 4 5 O GLU B 53  ? O GLU B 746 N THR B 32  ? N THR B 725 
AA3 5 6 O VAL B 33  ? O VAL B 726 N GLY B 26  ? N GLY B 719 
AA4 1 2 N LEU B 154 ? N LEU B 847 O LYS B 162 ? O LYS B 855 
# 
_pdbx_entry_details.entry_id                   9GC4 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     749 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NH2 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ARG 
_pdbx_validate_symm_contact.auth_seq_id_2     951 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_546 
_pdbx_validate_symm_contact.dist              2.14 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 736  ? ? -48.21  157.82  
2  1 PRO A 753  ? ? -86.08  32.07   
3  1 THR A 786  ? ? -120.01 -138.48 
4  1 ARG A 839  ? ? 77.36   -13.98  
5  1 ASP A 840  ? ? -142.56 46.86   
6  1 HIS A 873  ? ? -147.97 44.71   
7  1 ALA A 874  ? ? -88.52  47.30   
8  1 TRP A 954  ? ? -97.19  36.46   
9  1 GLU B 736  ? ? -48.68  157.37  
10 1 THR B 786  ? ? -131.14 -129.51 
11 1 ARG B 839  ? ? 77.79   -1.27   
12 1 ASP B 840  ? ? -153.63 45.17   
13 1 LEU B 865  ? ? -99.31  54.31   
14 1 ALA B 867  ? ? -138.55 -39.20  
15 1 HIS B 873  ? ? -149.73 39.16   
16 1 ALA B 874  ? ? -89.39  46.25   
17 1 TRP B 954  ? ? -97.22  36.15   
18 1 ASP D 1015 ? ? 72.70   48.39   
19 1 LEU D 1020 ? ? 91.56   104.06  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 1284 ? 11.23 . 
2 1 O ? B HOH 1285 ? 11.50 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A GLY 694  ? A GLY 1   
2   1 Y 1 A SER 695  ? A SER 2   
3   1 Y 1 A GLY 696  ? A GLY 3   
4   1 Y 1 A GLU 697  ? A GLU 4   
5   1 Y 1 A ALA 698  ? A ALA 5   
6   1 Y 1 A PRO 699  ? A PRO 6   
7   1 Y 1 A ASN 700  ? A ASN 7   
8   1 Y 1 A GLN 701  ? A GLN 8   
9   1 Y 1 A ALA 702  ? A ALA 9   
10  1 Y 1 A GLU 988  ? A GLU 295 
11  1 Y 1 A ARG 989  ? A ARG 296 
12  1 Y 1 A MET 990  ? A MET 297 
13  1 Y 1 A HIS 991  ? A HIS 298 
14  1 Y 1 A LEU 992  ? A LEU 299 
15  1 Y 1 A PRO 993  ? A PRO 300 
16  1 Y 1 A SER 994  ? A SER 301 
17  1 Y 1 A PRO 995  ? A PRO 302 
18  1 Y 1 A THR 996  ? A THR 303 
19  1 Y 1 A ASP 997  ? A ASP 304 
20  1 Y 1 A SER 998  ? A SER 305 
21  1 Y 1 A ASN 999  ? A ASN 306 
22  1 Y 1 A PHE 1000 ? A PHE 307 
23  1 Y 1 A TYR 1001 ? A TYR 308 
24  1 Y 1 A ARG 1002 ? A ARG 309 
25  1 Y 1 A ALA 1003 ? A ALA 310 
26  1 Y 1 A LEU 1004 ? A LEU 311 
27  1 Y 1 A MET 1005 ? A MET 312 
28  1 Y 1 A ASP 1006 ? A ASP 313 
29  1 Y 1 A GLU 1007 ? A GLU 314 
30  1 Y 1 A GLU 1008 ? A GLU 315 
31  1 Y 1 A ASP 1009 ? A ASP 316 
32  1 Y 1 A MET 1010 ? A MET 317 
33  1 Y 1 A ASP 1011 ? A ASP 318 
34  1 Y 1 A ASP 1012 ? A ASP 319 
35  1 Y 1 A VAL 1013 ? A VAL 320 
36  1 Y 1 A VAL 1014 ? A VAL 321 
37  1 Y 1 A ASP 1015 ? A ASP 322 
38  1 Y 1 A ALA 1016 ? A ALA 323 
39  1 Y 1 A ASP 1017 ? A ASP 324 
40  1 Y 1 A GLU 1018 ? A GLU 325 
41  1 Y 1 A TYR 1019 ? A TYR 326 
42  1 Y 1 A LEU 1020 ? A LEU 327 
43  1 Y 1 A ILE 1021 ? A ILE 328 
44  1 Y 1 A PRO 1022 ? A PRO 329 
45  1 Y 1 A GLN 1023 ? A GLN 330 
46  1 Y 1 A GLN 1024 ? A GLN 331 
47  1 Y 1 A GLY 1025 ? A GLY 332 
48  1 Y 1 B GLY 694  ? B GLY 1   
49  1 Y 1 B SER 695  ? B SER 2   
50  1 Y 1 B GLY 696  ? B GLY 3   
51  1 Y 1 B GLU 697  ? B GLU 4   
52  1 Y 1 B ALA 698  ? B ALA 5   
53  1 Y 1 B PRO 699  ? B PRO 6   
54  1 Y 1 B ASN 700  ? B ASN 7   
55  1 Y 1 B GLN 701  ? B GLN 8   
56  1 Y 1 B ALA 702  ? B ALA 9   
57  1 Y 1 B GLU 988  ? B GLU 295 
58  1 Y 1 B ARG 989  ? B ARG 296 
59  1 Y 1 B MET 990  ? B MET 297 
60  1 Y 1 B HIS 991  ? B HIS 298 
61  1 Y 1 B LEU 992  ? B LEU 299 
62  1 Y 1 B PRO 993  ? B PRO 300 
63  1 Y 1 B SER 994  ? B SER 301 
64  1 Y 1 B PRO 995  ? B PRO 302 
65  1 Y 1 B THR 996  ? B THR 303 
66  1 Y 1 B ASP 997  ? B ASP 304 
67  1 Y 1 B SER 998  ? B SER 305 
68  1 Y 1 B ASN 999  ? B ASN 306 
69  1 Y 1 B PHE 1000 ? B PHE 307 
70  1 Y 1 B TYR 1001 ? B TYR 308 
71  1 Y 1 B ARG 1002 ? B ARG 309 
72  1 Y 1 B ALA 1003 ? B ALA 310 
73  1 Y 1 B LEU 1004 ? B LEU 311 
74  1 Y 1 B MET 1005 ? B MET 312 
75  1 Y 1 B ASP 1006 ? B ASP 313 
76  1 Y 1 B GLU 1007 ? B GLU 314 
77  1 Y 1 B GLU 1008 ? B GLU 315 
78  1 Y 1 B ASP 1009 ? B ASP 316 
79  1 Y 1 B MET 1010 ? B MET 317 
80  1 Y 1 B ASP 1011 ? B ASP 318 
81  1 Y 1 B ASP 1012 ? B ASP 319 
82  1 Y 1 B VAL 1013 ? B VAL 320 
83  1 Y 1 B VAL 1014 ? B VAL 321 
84  1 Y 1 B ASP 1015 ? B ASP 322 
85  1 Y 1 B ALA 1016 ? B ALA 323 
86  1 Y 1 B ASP 1017 ? B ASP 324 
87  1 Y 1 B GLU 1018 ? B GLU 325 
88  1 Y 1 B TYR 1019 ? B TYR 326 
89  1 Y 1 B LEU 1020 ? B LEU 327 
90  1 Y 1 B ILE 1021 ? B ILE 328 
91  1 Y 1 B PRO 1022 ? B PRO 329 
92  1 Y 1 B GLN 1023 ? B GLN 330 
93  1 Y 1 B GLN 1024 ? B GLN 331 
94  1 Y 1 B GLY 1025 ? B GLY 332 
95  1 Y 1 D GLY 694  ? C GLY 1   
96  1 Y 1 D SER 695  ? C SER 2   
97  1 Y 1 D GLY 696  ? C GLY 3   
98  1 Y 1 D GLU 697  ? C GLU 4   
99  1 Y 1 D ALA 698  ? C ALA 5   
100 1 Y 1 D PRO 699  ? C PRO 6   
101 1 Y 1 D ASN 700  ? C ASN 7   
102 1 Y 1 D GLN 701  ? C GLN 8   
103 1 Y 1 D ALA 702  ? C ALA 9   
104 1 Y 1 D LEU 703  ? C LEU 10  
105 1 Y 1 D LEU 704  ? C LEU 11  
106 1 Y 1 D ARG 705  ? C ARG 12  
107 1 Y 1 D ILE 706  ? C ILE 13  
108 1 Y 1 D LEU 707  ? C LEU 14  
109 1 Y 1 D LYS 708  ? C LYS 15  
110 1 Y 1 D GLU 709  ? C GLU 16  
111 1 Y 1 D THR 710  ? C THR 17  
112 1 Y 1 D GLU 711  ? C GLU 18  
113 1 Y 1 D PHE 712  ? C PHE 19  
114 1 Y 1 D LYS 713  ? C LYS 20  
115 1 Y 1 D LYS 714  ? C LYS 21  
116 1 Y 1 D ILE 715  ? C ILE 22  
117 1 Y 1 D LYS 716  ? C LYS 23  
118 1 Y 1 D VAL 717  ? C VAL 24  
119 1 Y 1 D LEU 718  ? C LEU 25  
120 1 Y 1 D GLY 719  ? C GLY 26  
121 1 Y 1 D SER 720  ? C SER 27  
122 1 Y 1 D GLY 721  ? C GLY 28  
123 1 Y 1 D ALA 722  ? C ALA 29  
124 1 Y 1 D PHE 723  ? C PHE 30  
125 1 Y 1 D GLY 724  ? C GLY 31  
126 1 Y 1 D THR 725  ? C THR 32  
127 1 Y 1 D VAL 726  ? C VAL 33  
128 1 Y 1 D TYR 727  ? C TYR 34  
129 1 Y 1 D LYS 728  ? C LYS 35  
130 1 Y 1 D GLY 729  ? C GLY 36  
131 1 Y 1 D LEU 730  ? C LEU 37  
132 1 Y 1 D TRP 731  ? C TRP 38  
133 1 Y 1 D ILE 732  ? C ILE 39  
134 1 Y 1 D PRO 733  ? C PRO 40  
135 1 Y 1 D GLU 734  ? C GLU 41  
136 1 Y 1 D GLY 735  ? C GLY 42  
137 1 Y 1 D GLU 736  ? C GLU 43  
138 1 Y 1 D LYS 737  ? C LYS 44  
139 1 Y 1 D VAL 738  ? C VAL 45  
140 1 Y 1 D LYS 739  ? C LYS 46  
141 1 Y 1 D ILE 740  ? C ILE 47  
142 1 Y 1 D PRO 741  ? C PRO 48  
143 1 Y 1 D VAL 742  ? C VAL 49  
144 1 Y 1 D ALA 743  ? C ALA 50  
145 1 Y 1 D ILE 744  ? C ILE 51  
146 1 Y 1 D LYS 745  ? C LYS 52  
147 1 Y 1 D GLU 746  ? C GLU 53  
148 1 Y 1 D LEU 747  ? C LEU 54  
149 1 Y 1 D ARG 748  ? C ARG 55  
150 1 Y 1 D GLU 749  ? C GLU 56  
151 1 Y 1 D ALA 750  ? C ALA 57  
152 1 Y 1 D THR 751  ? C THR 58  
153 1 Y 1 D SER 752  ? C SER 59  
154 1 Y 1 D PRO 753  ? C PRO 60  
155 1 Y 1 D LYS 754  ? C LYS 61  
156 1 Y 1 D ALA 755  ? C ALA 62  
157 1 Y 1 D ASN 756  ? C ASN 63  
158 1 Y 1 D LYS 757  ? C LYS 64  
159 1 Y 1 D GLU 758  ? C GLU 65  
160 1 Y 1 D ILE 759  ? C ILE 66  
161 1 Y 1 D LEU 760  ? C LEU 67  
162 1 Y 1 D ASP 761  ? C ASP 68  
163 1 Y 1 D GLU 762  ? C GLU 69  
164 1 Y 1 D ALA 763  ? C ALA 70  
165 1 Y 1 D TYR 764  ? C TYR 71  
166 1 Y 1 D VAL 765  ? C VAL 72  
167 1 Y 1 D MET 766  ? C MET 73  
168 1 Y 1 D ALA 767  ? C ALA 74  
169 1 Y 1 D SER 768  ? C SER 75  
170 1 Y 1 D VAL 769  ? C VAL 76  
171 1 Y 1 D ASP 770  ? C ASP 77  
172 1 Y 1 D ASN 771  ? C ASN 78  
173 1 Y 1 D PRO 772  ? C PRO 79  
174 1 Y 1 D GLY 773  ? C GLY 80  
175 1 Y 1 D ASN 774  ? C ASN 81  
176 1 Y 1 D PRO 775  ? C PRO 82  
177 1 Y 1 D HIS 776  ? C HIS 83  
178 1 Y 1 D VAL 777  ? C VAL 84  
179 1 Y 1 D CYS 778  ? C CYS 85  
180 1 Y 1 D ARG 779  ? C ARG 86  
181 1 Y 1 D LEU 780  ? C LEU 87  
182 1 Y 1 D LEU 781  ? C LEU 88  
183 1 Y 1 D GLY 782  ? C GLY 89  
184 1 Y 1 D ILE 783  ? C ILE 90  
185 1 Y 1 D CYS 784  ? C CYS 91  
186 1 Y 1 D LEU 785  ? C LEU 92  
187 1 Y 1 D THR 786  ? C THR 93  
188 1 Y 1 D SER 787  ? C SER 94  
189 1 Y 1 D THR 788  ? C THR 95  
190 1 Y 1 D VAL 789  ? C VAL 96  
191 1 Y 1 D GLN 790  ? C GLN 97  
192 1 Y 1 D LEU 791  ? C LEU 98  
193 1 Y 1 D ILE 792  ? C ILE 99  
194 1 Y 1 D THR 793  ? C THR 100 
195 1 Y 1 D GLN 794  ? C GLN 101 
196 1 Y 1 D LEU 795  ? C LEU 102 
197 1 Y 1 D MET 796  ? C MET 103 
198 1 Y 1 D PRO 797  ? C PRO 104 
199 1 Y 1 D PHE 798  ? C PHE 105 
200 1 Y 1 D GLY 799  ? C GLY 106 
201 1 Y 1 D CYS 800  ? C CYS 107 
202 1 Y 1 D LEU 801  ? C LEU 108 
203 1 Y 1 D LEU 802  ? C LEU 109 
204 1 Y 1 D ASP 803  ? C ASP 110 
205 1 Y 1 D TYR 804  ? C TYR 111 
206 1 Y 1 D VAL 805  ? C VAL 112 
207 1 Y 1 D ARG 806  ? C ARG 113 
208 1 Y 1 D GLU 807  ? C GLU 114 
209 1 Y 1 D HIS 808  ? C HIS 115 
210 1 Y 1 D LYS 809  ? C LYS 116 
211 1 Y 1 D ASP 810  ? C ASP 117 
212 1 Y 1 D ASN 811  ? C ASN 118 
213 1 Y 1 D ILE 812  ? C ILE 119 
214 1 Y 1 D GLY 813  ? C GLY 120 
215 1 Y 1 D SER 814  ? C SER 121 
216 1 Y 1 D GLN 815  ? C GLN 122 
217 1 Y 1 D TYR 816  ? C TYR 123 
218 1 Y 1 D LEU 817  ? C LEU 124 
219 1 Y 1 D LEU 818  ? C LEU 125 
220 1 Y 1 D ASN 819  ? C ASN 126 
221 1 Y 1 D TRP 820  ? C TRP 127 
222 1 Y 1 D CYS 821  ? C CYS 128 
223 1 Y 1 D VAL 822  ? C VAL 129 
224 1 Y 1 D GLN 823  ? C GLN 130 
225 1 Y 1 D ILE 824  ? C ILE 131 
226 1 Y 1 D ALA 825  ? C ALA 132 
227 1 Y 1 D LYS 826  ? C LYS 133 
228 1 Y 1 D GLY 827  ? C GLY 134 
229 1 Y 1 D MET 828  ? C MET 135 
230 1 Y 1 D ASN 829  ? C ASN 136 
231 1 Y 1 D TYR 830  ? C TYR 137 
232 1 Y 1 D LEU 831  ? C LEU 138 
233 1 Y 1 D GLU 832  ? C GLU 139 
234 1 Y 1 D ASP 833  ? C ASP 140 
235 1 Y 1 D ARG 834  ? C ARG 141 
236 1 Y 1 D ARG 835  ? C ARG 142 
237 1 Y 1 D LEU 836  ? C LEU 143 
238 1 Y 1 D VAL 837  ? C VAL 144 
239 1 Y 1 D HIS 838  ? C HIS 145 
240 1 Y 1 D ARG 839  ? C ARG 146 
241 1 Y 1 D ASP 840  ? C ASP 147 
242 1 Y 1 D LEU 841  ? C LEU 148 
243 1 Y 1 D ALA 842  ? C ALA 149 
244 1 Y 1 D ALA 843  ? C ALA 150 
245 1 Y 1 D ARG 844  ? C ARG 151 
246 1 Y 1 D ASN 845  ? C ASN 152 
247 1 Y 1 D VAL 846  ? C VAL 153 
248 1 Y 1 D LEU 847  ? C LEU 154 
249 1 Y 1 D VAL 848  ? C VAL 155 
250 1 Y 1 D LYS 849  ? C LYS 156 
251 1 Y 1 D THR 850  ? C THR 157 
252 1 Y 1 D PRO 851  ? C PRO 158 
253 1 Y 1 D GLN 852  ? C GLN 159 
254 1 Y 1 D HIS 853  ? C HIS 160 
255 1 Y 1 D VAL 854  ? C VAL 161 
256 1 Y 1 D LYS 855  ? C LYS 162 
257 1 Y 1 D ILE 856  ? C ILE 163 
258 1 Y 1 D THR 857  ? C THR 164 
259 1 Y 1 D ASP 858  ? C ASP 165 
260 1 Y 1 D PHE 859  ? C PHE 166 
261 1 Y 1 D GLY 860  ? C GLY 167 
262 1 Y 1 D LEU 861  ? C LEU 168 
263 1 Y 1 D ALA 862  ? C ALA 169 
264 1 Y 1 D LYS 863  ? C LYS 170 
265 1 Y 1 D LEU 864  ? C LEU 171 
266 1 Y 1 D LEU 865  ? C LEU 172 
267 1 Y 1 D GLY 866  ? C GLY 173 
268 1 Y 1 D ALA 867  ? C ALA 174 
269 1 Y 1 D GLU 868  ? C GLU 175 
270 1 Y 1 D GLU 869  ? C GLU 176 
271 1 Y 1 D LYS 870  ? C LYS 177 
272 1 Y 1 D GLU 871  ? C GLU 178 
273 1 Y 1 D TYR 872  ? C TYR 179 
274 1 Y 1 D HIS 873  ? C HIS 180 
275 1 Y 1 D ALA 874  ? C ALA 181 
276 1 Y 1 D GLU 875  ? C GLU 182 
277 1 Y 1 D GLY 876  ? C GLY 183 
278 1 Y 1 D GLY 877  ? C GLY 184 
279 1 Y 1 D LYS 878  ? C LYS 185 
280 1 Y 1 D VAL 879  ? C VAL 186 
281 1 Y 1 D PRO 880  ? C PRO 187 
282 1 Y 1 D ILE 881  ? C ILE 188 
283 1 Y 1 D LYS 882  ? C LYS 189 
284 1 Y 1 D TRP 883  ? C TRP 190 
285 1 Y 1 D MET 884  ? C MET 191 
286 1 Y 1 D ALA 885  ? C ALA 192 
287 1 Y 1 D LEU 886  ? C LEU 193 
288 1 Y 1 D GLU 887  ? C GLU 194 
289 1 Y 1 D SER 888  ? C SER 195 
290 1 Y 1 D ILE 889  ? C ILE 196 
291 1 Y 1 D LEU 890  ? C LEU 197 
292 1 Y 1 D HIS 891  ? C HIS 198 
293 1 Y 1 D ARG 892  ? C ARG 199 
294 1 Y 1 D ILE 893  ? C ILE 200 
295 1 Y 1 D TYR 894  ? C TYR 201 
296 1 Y 1 D THR 895  ? C THR 202 
297 1 Y 1 D HIS 896  ? C HIS 203 
298 1 Y 1 D GLN 897  ? C GLN 204 
299 1 Y 1 D SER 898  ? C SER 205 
300 1 Y 1 D ASP 899  ? C ASP 206 
301 1 Y 1 D VAL 900  ? C VAL 207 
302 1 Y 1 D TRP 901  ? C TRP 208 
303 1 Y 1 D SER 902  ? C SER 209 
304 1 Y 1 D TYR 903  ? C TYR 210 
305 1 Y 1 D GLY 904  ? C GLY 211 
306 1 Y 1 D VAL 905  ? C VAL 212 
307 1 Y 1 D THR 906  ? C THR 213 
308 1 Y 1 D VAL 907  ? C VAL 214 
309 1 Y 1 D TRP 908  ? C TRP 215 
310 1 Y 1 D GLU 909  ? C GLU 216 
311 1 Y 1 D LEU 910  ? C LEU 217 
312 1 Y 1 D MET 911  ? C MET 218 
313 1 Y 1 D THR 912  ? C THR 219 
314 1 Y 1 D PHE 913  ? C PHE 220 
315 1 Y 1 D GLY 914  ? C GLY 221 
316 1 Y 1 D SER 915  ? C SER 222 
317 1 Y 1 D LYS 916  ? C LYS 223 
318 1 Y 1 D PRO 917  ? C PRO 224 
319 1 Y 1 D TYR 918  ? C TYR 225 
320 1 Y 1 D ASP 919  ? C ASP 226 
321 1 Y 1 D GLY 920  ? C GLY 227 
322 1 Y 1 D ILE 921  ? C ILE 228 
323 1 Y 1 D PRO 922  ? C PRO 229 
324 1 Y 1 D ALA 923  ? C ALA 230 
325 1 Y 1 D SER 924  ? C SER 231 
326 1 Y 1 D GLU 925  ? C GLU 232 
327 1 Y 1 D ILE 926  ? C ILE 233 
328 1 Y 1 D SER 927  ? C SER 234 
329 1 Y 1 D SER 928  ? C SER 235 
330 1 Y 1 D ILE 929  ? C ILE 236 
331 1 Y 1 D LEU 930  ? C LEU 237 
332 1 Y 1 D GLU 931  ? C GLU 238 
333 1 Y 1 D LYS 932  ? C LYS 239 
334 1 Y 1 D GLY 933  ? C GLY 240 
335 1 Y 1 D GLU 934  ? C GLU 241 
336 1 Y 1 D ARG 935  ? C ARG 242 
337 1 Y 1 D LEU 936  ? C LEU 243 
338 1 Y 1 D PRO 937  ? C PRO 244 
339 1 Y 1 D GLN 938  ? C GLN 245 
340 1 Y 1 D PRO 939  ? C PRO 246 
341 1 Y 1 D PRO 940  ? C PRO 247 
342 1 Y 1 D ILE 941  ? C ILE 248 
343 1 Y 1 D CYS 942  ? C CYS 249 
344 1 Y 1 D THR 943  ? C THR 250 
345 1 Y 1 D ILE 944  ? C ILE 251 
346 1 Y 1 D ASP 945  ? C ASP 252 
347 1 Y 1 D VAL 946  ? C VAL 253 
348 1 Y 1 D TYR 947  ? C TYR 254 
349 1 Y 1 D MET 948  ? C MET 255 
350 1 Y 1 D ILE 949  ? C ILE 256 
351 1 Y 1 D MET 950  ? C MET 257 
352 1 Y 1 D ARG 951  ? C ARG 258 
353 1 Y 1 D LYS 952  ? C LYS 259 
354 1 Y 1 D CYS 953  ? C CYS 260 
355 1 Y 1 D TRP 954  ? C TRP 261 
356 1 Y 1 D MET 955  ? C MET 262 
357 1 Y 1 D ILE 956  ? C ILE 263 
358 1 Y 1 D ASP 957  ? C ASP 264 
359 1 Y 1 D ALA 958  ? C ALA 265 
360 1 Y 1 D ASP 959  ? C ASP 266 
361 1 Y 1 D SER 960  ? C SER 267 
362 1 Y 1 D ARG 961  ? C ARG 268 
363 1 Y 1 D PRO 962  ? C PRO 269 
364 1 Y 1 D LYS 963  ? C LYS 270 
365 1 Y 1 D PHE 964  ? C PHE 271 
366 1 Y 1 D ARG 965  ? C ARG 272 
367 1 Y 1 D GLU 966  ? C GLU 273 
368 1 Y 1 D LEU 967  ? C LEU 274 
369 1 Y 1 D ILE 968  ? C ILE 275 
370 1 Y 1 D ILE 969  ? C ILE 276 
371 1 Y 1 D GLU 970  ? C GLU 277 
372 1 Y 1 D PHE 971  ? C PHE 278 
373 1 Y 1 D SER 972  ? C SER 279 
374 1 Y 1 D LYS 973  ? C LYS 280 
375 1 Y 1 D MET 974  ? C MET 281 
376 1 Y 1 D ALA 975  ? C ALA 282 
377 1 Y 1 D ARG 976  ? C ARG 283 
378 1 Y 1 D ASP 977  ? C ASP 284 
379 1 Y 1 D PRO 978  ? C PRO 285 
380 1 Y 1 D GLN 979  ? C GLN 286 
381 1 Y 1 D ARG 980  ? C ARG 287 
382 1 Y 1 D TYR 981  ? C TYR 288 
383 1 Y 1 D LEU 982  ? C LEU 289 
384 1 Y 1 D VAL 983  ? C VAL 290 
385 1 Y 1 D ILE 984  ? C ILE 291 
386 1 Y 1 D GLN 985  ? C GLN 292 
387 1 Y 1 D GLY 986  ? C GLY 293 
388 1 Y 1 D ASP 987  ? C ASP 294 
389 1 Y 1 D GLU 988  ? C GLU 295 
390 1 Y 1 D ARG 989  ? C ARG 296 
391 1 Y 1 D MET 990  ? C MET 297 
392 1 Y 1 D HIS 991  ? C HIS 298 
393 1 Y 1 D LEU 992  ? C LEU 299 
394 1 Y 1 D PRO 993  ? C PRO 300 
395 1 Y 1 D SER 994  ? C SER 301 
396 1 Y 1 D PRO 995  ? C PRO 302 
397 1 Y 1 D THR 996  ? C THR 303 
398 1 Y 1 D ASP 997  ? C ASP 304 
399 1 Y 1 D SER 998  ? C SER 305 
400 1 Y 1 D ASN 999  ? C ASN 306 
401 1 Y 1 D PHE 1000 ? C PHE 307 
402 1 Y 1 D TYR 1001 ? C TYR 308 
403 1 Y 1 D ARG 1002 ? C ARG 309 
404 1 Y 1 D ALA 1003 ? C ALA 310 
405 1 Y 1 D LEU 1004 ? C LEU 311 
406 1 Y 1 D PRO 1022 ? C PRO 329 
407 1 Y 1 D GLN 1023 ? C GLN 330 
408 1 Y 1 D GLN 1024 ? C GLN 331 
409 1 Y 1 D GLY 1025 ? C GLY 332 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1IZ7 C1   C  Y N 1   
A1IZ7 C2   C  Y N 2   
A1IZ7 C3   C  Y N 3   
A1IZ7 C7   C  Y N 4   
A1IZ7 C8   C  Y N 5   
A1IZ7 C9   C  Y N 6   
A1IZ7 C10  C  Y N 7   
A1IZ7 C11  C  Y N 8   
A1IZ7 C12  C  Y N 9   
A1IZ7 C13  C  N N 10  
A1IZ7 C14  C  N N 11  
A1IZ7 C15  C  Y N 12  
A1IZ7 C16  C  Y N 13  
A1IZ7 C19  C  Y N 14  
A1IZ7 C20  C  N N 15  
A1IZ7 C21  C  N N 16  
A1IZ7 C22  C  N N 17  
A1IZ7 O1   O  N N 18  
A1IZ7 N1   N  N N 19  
A1IZ7 N    N  Y N 20  
A1IZ7 N2   N  Y N 21  
A1IZ7 N4   N  Y N 22  
A1IZ7 N3   N  Y N 23  
A1IZ7 C18  C  Y N 24  
A1IZ7 C17  C  Y N 25  
A1IZ7 C6   C  Y N 26  
A1IZ7 C5   C  Y N 27  
A1IZ7 O    O  N N 28  
A1IZ7 C4   C  Y N 29  
A1IZ7 N5   N  Y N 30  
A1IZ7 C    C  Y N 31  
A1IZ7 F    F  N N 32  
A1IZ7 CL   CL N N 33  
A1IZ7 H1   H  N N 34  
A1IZ7 H2   H  N N 35  
A1IZ7 H3   H  N N 36  
A1IZ7 H4   H  N N 37  
A1IZ7 H5   H  N N 38  
A1IZ7 H8   H  N N 39  
A1IZ7 H9   H  N N 40  
A1IZ7 H10  H  N N 41  
A1IZ7 H11  H  N N 42  
A1IZ7 H12  H  N N 43  
A1IZ7 H13  H  N N 44  
A1IZ7 H14  H  N N 45  
A1IZ7 H15  H  N N 46  
A1IZ7 H16  H  N N 47  
A1IZ7 H6   H  N N 48  
A1IZ7 H7   H  N N 49  
A1IZ7 H17  H  N N 50  
A1IZ7 H18  H  N N 51  
ALA   N    N  N N 52  
ALA   CA   C  N S 53  
ALA   C    C  N N 54  
ALA   O    O  N N 55  
ALA   CB   C  N N 56  
ALA   OXT  O  N N 57  
ALA   H    H  N N 58  
ALA   H2   H  N N 59  
ALA   HA   H  N N 60  
ALA   HB1  H  N N 61  
ALA   HB2  H  N N 62  
ALA   HB3  H  N N 63  
ALA   HXT  H  N N 64  
ARG   N    N  N N 65  
ARG   CA   C  N S 66  
ARG   C    C  N N 67  
ARG   O    O  N N 68  
ARG   CB   C  N N 69  
ARG   CG   C  N N 70  
ARG   CD   C  N N 71  
ARG   NE   N  N N 72  
ARG   CZ   C  N N 73  
ARG   NH1  N  N N 74  
ARG   NH2  N  N N 75  
ARG   OXT  O  N N 76  
ARG   H    H  N N 77  
ARG   H2   H  N N 78  
ARG   HA   H  N N 79  
ARG   HB2  H  N N 80  
ARG   HB3  H  N N 81  
ARG   HG2  H  N N 82  
ARG   HG3  H  N N 83  
ARG   HD2  H  N N 84  
ARG   HD3  H  N N 85  
ARG   HE   H  N N 86  
ARG   HH11 H  N N 87  
ARG   HH12 H  N N 88  
ARG   HH21 H  N N 89  
ARG   HH22 H  N N 90  
ARG   HXT  H  N N 91  
ASN   N    N  N N 92  
ASN   CA   C  N S 93  
ASN   C    C  N N 94  
ASN   O    O  N N 95  
ASN   CB   C  N N 96  
ASN   CG   C  N N 97  
ASN   OD1  O  N N 98  
ASN   ND2  N  N N 99  
ASN   OXT  O  N N 100 
ASN   H    H  N N 101 
ASN   H2   H  N N 102 
ASN   HA   H  N N 103 
ASN   HB2  H  N N 104 
ASN   HB3  H  N N 105 
ASN   HD21 H  N N 106 
ASN   HD22 H  N N 107 
ASN   HXT  H  N N 108 
ASP   N    N  N N 109 
ASP   CA   C  N S 110 
ASP   C    C  N N 111 
ASP   O    O  N N 112 
ASP   CB   C  N N 113 
ASP   CG   C  N N 114 
ASP   OD1  O  N N 115 
ASP   OD2  O  N N 116 
ASP   OXT  O  N N 117 
ASP   H    H  N N 118 
ASP   H2   H  N N 119 
ASP   HA   H  N N 120 
ASP   HB2  H  N N 121 
ASP   HB3  H  N N 122 
ASP   HD2  H  N N 123 
ASP   HXT  H  N N 124 
CYS   N    N  N N 125 
CYS   CA   C  N R 126 
CYS   C    C  N N 127 
CYS   O    O  N N 128 
CYS   CB   C  N N 129 
CYS   SG   S  N N 130 
CYS   OXT  O  N N 131 
CYS   H    H  N N 132 
CYS   H2   H  N N 133 
CYS   HA   H  N N 134 
CYS   HB2  H  N N 135 
CYS   HB3  H  N N 136 
CYS   HG   H  N N 137 
CYS   HXT  H  N N 138 
GLN   N    N  N N 139 
GLN   CA   C  N S 140 
GLN   C    C  N N 141 
GLN   O    O  N N 142 
GLN   CB   C  N N 143 
GLN   CG   C  N N 144 
GLN   CD   C  N N 145 
GLN   OE1  O  N N 146 
GLN   NE2  N  N N 147 
GLN   OXT  O  N N 148 
GLN   H    H  N N 149 
GLN   H2   H  N N 150 
GLN   HA   H  N N 151 
GLN   HB2  H  N N 152 
GLN   HB3  H  N N 153 
GLN   HG2  H  N N 154 
GLN   HG3  H  N N 155 
GLN   HE21 H  N N 156 
GLN   HE22 H  N N 157 
GLN   HXT  H  N N 158 
GLU   N    N  N N 159 
GLU   CA   C  N S 160 
GLU   C    C  N N 161 
GLU   O    O  N N 162 
GLU   CB   C  N N 163 
GLU   CG   C  N N 164 
GLU   CD   C  N N 165 
GLU   OE1  O  N N 166 
GLU   OE2  O  N N 167 
GLU   OXT  O  N N 168 
GLU   H    H  N N 169 
GLU   H2   H  N N 170 
GLU   HA   H  N N 171 
GLU   HB2  H  N N 172 
GLU   HB3  H  N N 173 
GLU   HG2  H  N N 174 
GLU   HG3  H  N N 175 
GLU   HE2  H  N N 176 
GLU   HXT  H  N N 177 
GLY   N    N  N N 178 
GLY   CA   C  N N 179 
GLY   C    C  N N 180 
GLY   O    O  N N 181 
GLY   OXT  O  N N 182 
GLY   H    H  N N 183 
GLY   H2   H  N N 184 
GLY   HA2  H  N N 185 
GLY   HA3  H  N N 186 
GLY   HXT  H  N N 187 
HIS   N    N  N N 188 
HIS   CA   C  N S 189 
HIS   C    C  N N 190 
HIS   O    O  N N 191 
HIS   CB   C  N N 192 
HIS   CG   C  Y N 193 
HIS   ND1  N  Y N 194 
HIS   CD2  C  Y N 195 
HIS   CE1  C  Y N 196 
HIS   NE2  N  Y N 197 
HIS   OXT  O  N N 198 
HIS   H    H  N N 199 
HIS   H2   H  N N 200 
HIS   HA   H  N N 201 
HIS   HB2  H  N N 202 
HIS   HB3  H  N N 203 
HIS   HD1  H  N N 204 
HIS   HD2  H  N N 205 
HIS   HE1  H  N N 206 
HIS   HE2  H  N N 207 
HIS   HXT  H  N N 208 
HOH   O    O  N N 209 
HOH   H1   H  N N 210 
HOH   H2   H  N N 211 
ILE   N    N  N N 212 
ILE   CA   C  N S 213 
ILE   C    C  N N 214 
ILE   O    O  N N 215 
ILE   CB   C  N S 216 
ILE   CG1  C  N N 217 
ILE   CG2  C  N N 218 
ILE   CD1  C  N N 219 
ILE   OXT  O  N N 220 
ILE   H    H  N N 221 
ILE   H2   H  N N 222 
ILE   HA   H  N N 223 
ILE   HB   H  N N 224 
ILE   HG12 H  N N 225 
ILE   HG13 H  N N 226 
ILE   HG21 H  N N 227 
ILE   HG22 H  N N 228 
ILE   HG23 H  N N 229 
ILE   HD11 H  N N 230 
ILE   HD12 H  N N 231 
ILE   HD13 H  N N 232 
ILE   HXT  H  N N 233 
LEU   N    N  N N 234 
LEU   CA   C  N S 235 
LEU   C    C  N N 236 
LEU   O    O  N N 237 
LEU   CB   C  N N 238 
LEU   CG   C  N N 239 
LEU   CD1  C  N N 240 
LEU   CD2  C  N N 241 
LEU   OXT  O  N N 242 
LEU   H    H  N N 243 
LEU   H2   H  N N 244 
LEU   HA   H  N N 245 
LEU   HB2  H  N N 246 
LEU   HB3  H  N N 247 
LEU   HG   H  N N 248 
LEU   HD11 H  N N 249 
LEU   HD12 H  N N 250 
LEU   HD13 H  N N 251 
LEU   HD21 H  N N 252 
LEU   HD22 H  N N 253 
LEU   HD23 H  N N 254 
LEU   HXT  H  N N 255 
LYS   N    N  N N 256 
LYS   CA   C  N S 257 
LYS   C    C  N N 258 
LYS   O    O  N N 259 
LYS   CB   C  N N 260 
LYS   CG   C  N N 261 
LYS   CD   C  N N 262 
LYS   CE   C  N N 263 
LYS   NZ   N  N N 264 
LYS   OXT  O  N N 265 
LYS   H    H  N N 266 
LYS   H2   H  N N 267 
LYS   HA   H  N N 268 
LYS   HB2  H  N N 269 
LYS   HB3  H  N N 270 
LYS   HG2  H  N N 271 
LYS   HG3  H  N N 272 
LYS   HD2  H  N N 273 
LYS   HD3  H  N N 274 
LYS   HE2  H  N N 275 
LYS   HE3  H  N N 276 
LYS   HZ1  H  N N 277 
LYS   HZ2  H  N N 278 
LYS   HZ3  H  N N 279 
LYS   HXT  H  N N 280 
MET   N    N  N N 281 
MET   CA   C  N S 282 
MET   C    C  N N 283 
MET   O    O  N N 284 
MET   CB   C  N N 285 
MET   CG   C  N N 286 
MET   SD   S  N N 287 
MET   CE   C  N N 288 
MET   OXT  O  N N 289 
MET   H    H  N N 290 
MET   H2   H  N N 291 
MET   HA   H  N N 292 
MET   HB2  H  N N 293 
MET   HB3  H  N N 294 
MET   HG2  H  N N 295 
MET   HG3  H  N N 296 
MET   HE1  H  N N 297 
MET   HE2  H  N N 298 
MET   HE3  H  N N 299 
MET   HXT  H  N N 300 
PHE   N    N  N N 301 
PHE   CA   C  N S 302 
PHE   C    C  N N 303 
PHE   O    O  N N 304 
PHE   CB   C  N N 305 
PHE   CG   C  Y N 306 
PHE   CD1  C  Y N 307 
PHE   CD2  C  Y N 308 
PHE   CE1  C  Y N 309 
PHE   CE2  C  Y N 310 
PHE   CZ   C  Y N 311 
PHE   OXT  O  N N 312 
PHE   H    H  N N 313 
PHE   H2   H  N N 314 
PHE   HA   H  N N 315 
PHE   HB2  H  N N 316 
PHE   HB3  H  N N 317 
PHE   HD1  H  N N 318 
PHE   HD2  H  N N 319 
PHE   HE1  H  N N 320 
PHE   HE2  H  N N 321 
PHE   HZ   H  N N 322 
PHE   HXT  H  N N 323 
PRO   N    N  N N 324 
PRO   CA   C  N S 325 
PRO   C    C  N N 326 
PRO   O    O  N N 327 
PRO   CB   C  N N 328 
PRO   CG   C  N N 329 
PRO   CD   C  N N 330 
PRO   OXT  O  N N 331 
PRO   H    H  N N 332 
PRO   HA   H  N N 333 
PRO   HB2  H  N N 334 
PRO   HB3  H  N N 335 
PRO   HG2  H  N N 336 
PRO   HG3  H  N N 337 
PRO   HD2  H  N N 338 
PRO   HD3  H  N N 339 
PRO   HXT  H  N N 340 
SER   N    N  N N 341 
SER   CA   C  N S 342 
SER   C    C  N N 343 
SER   O    O  N N 344 
SER   CB   C  N N 345 
SER   OG   O  N N 346 
SER   OXT  O  N N 347 
SER   H    H  N N 348 
SER   H2   H  N N 349 
SER   HA   H  N N 350 
SER   HB2  H  N N 351 
SER   HB3  H  N N 352 
SER   HG   H  N N 353 
SER   HXT  H  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1IZ7 C1  C2   doub Y N 1   
A1IZ7 C1  C    sing Y N 2   
A1IZ7 F   C    sing N N 3   
A1IZ7 C2  C3   sing Y N 4   
A1IZ7 C   N5   doub Y N 5   
A1IZ7 N5  C4   sing Y N 6   
A1IZ7 C3  C4   doub Y N 7   
A1IZ7 C3  CL   sing N N 8   
A1IZ7 C4  O    sing N N 9   
A1IZ7 O   C5   sing N N 10  
A1IZ7 C6  C5   doub Y N 11  
A1IZ7 C6  C7   sing Y N 12  
A1IZ7 C5  C10  sing Y N 13  
A1IZ7 C7  C8   doub Y N 14  
A1IZ7 C10 C9   doub Y N 15  
A1IZ7 C8  C9   sing Y N 16  
A1IZ7 C9  C11  sing N N 17  
A1IZ7 C19 N4   doub Y N 18  
A1IZ7 C19 N3   sing Y N 19  
A1IZ7 N4  C16  sing Y N 20  
A1IZ7 N3  C18  doub Y N 21  
A1IZ7 C11 N2   sing Y N 22  
A1IZ7 C11 N    doub Y N 23  
A1IZ7 C16 N2   sing N N 24  
A1IZ7 C16 C17  doub Y N 25  
A1IZ7 N2  C15  sing Y N 26  
A1IZ7 N   C12  sing Y N 27  
A1IZ7 C18 C17  sing Y N 28  
A1IZ7 C15 C12  doub Y N 29  
A1IZ7 C15 C14  sing N N 30  
A1IZ7 C12 C13  sing N N 31  
A1IZ7 C14 N1   sing N N 32  
A1IZ7 C13 N1   sing N N 33  
A1IZ7 N1  C20  sing N N 34  
A1IZ7 C20 O1   doub N N 35  
A1IZ7 C20 C21  sing N N 36  
A1IZ7 C21 C22  sing N N 37  
A1IZ7 C1  H1   sing N N 38  
A1IZ7 C2  H2   sing N N 39  
A1IZ7 C7  H3   sing N N 40  
A1IZ7 C8  H4   sing N N 41  
A1IZ7 C10 H5   sing N N 42  
A1IZ7 C19 H8   sing N N 43  
A1IZ7 C21 H9   sing N N 44  
A1IZ7 C21 H10  sing N N 45  
A1IZ7 C22 H11  sing N N 46  
A1IZ7 C22 H12  sing N N 47  
A1IZ7 C22 H13  sing N N 48  
A1IZ7 C18 H14  sing N N 49  
A1IZ7 C17 H15  sing N N 50  
A1IZ7 C6  H16  sing N N 51  
A1IZ7 C13 H6   sing N N 52  
A1IZ7 C13 H7   sing N N 53  
A1IZ7 C14 H17  sing N N 54  
A1IZ7 C14 H18  sing N N 55  
ALA   N   CA   sing N N 56  
ALA   N   H    sing N N 57  
ALA   N   H2   sing N N 58  
ALA   CA  C    sing N N 59  
ALA   CA  CB   sing N N 60  
ALA   CA  HA   sing N N 61  
ALA   C   O    doub N N 62  
ALA   C   OXT  sing N N 63  
ALA   CB  HB1  sing N N 64  
ALA   CB  HB2  sing N N 65  
ALA   CB  HB3  sing N N 66  
ALA   OXT HXT  sing N N 67  
ARG   N   CA   sing N N 68  
ARG   N   H    sing N N 69  
ARG   N   H2   sing N N 70  
ARG   CA  C    sing N N 71  
ARG   CA  CB   sing N N 72  
ARG   CA  HA   sing N N 73  
ARG   C   O    doub N N 74  
ARG   C   OXT  sing N N 75  
ARG   CB  CG   sing N N 76  
ARG   CB  HB2  sing N N 77  
ARG   CB  HB3  sing N N 78  
ARG   CG  CD   sing N N 79  
ARG   CG  HG2  sing N N 80  
ARG   CG  HG3  sing N N 81  
ARG   CD  NE   sing N N 82  
ARG   CD  HD2  sing N N 83  
ARG   CD  HD3  sing N N 84  
ARG   NE  CZ   sing N N 85  
ARG   NE  HE   sing N N 86  
ARG   CZ  NH1  sing N N 87  
ARG   CZ  NH2  doub N N 88  
ARG   NH1 HH11 sing N N 89  
ARG   NH1 HH12 sing N N 90  
ARG   NH2 HH21 sing N N 91  
ARG   NH2 HH22 sing N N 92  
ARG   OXT HXT  sing N N 93  
ASN   N   CA   sing N N 94  
ASN   N   H    sing N N 95  
ASN   N   H2   sing N N 96  
ASN   CA  C    sing N N 97  
ASN   CA  CB   sing N N 98  
ASN   CA  HA   sing N N 99  
ASN   C   O    doub N N 100 
ASN   C   OXT  sing N N 101 
ASN   CB  CG   sing N N 102 
ASN   CB  HB2  sing N N 103 
ASN   CB  HB3  sing N N 104 
ASN   CG  OD1  doub N N 105 
ASN   CG  ND2  sing N N 106 
ASN   ND2 HD21 sing N N 107 
ASN   ND2 HD22 sing N N 108 
ASN   OXT HXT  sing N N 109 
ASP   N   CA   sing N N 110 
ASP   N   H    sing N N 111 
ASP   N   H2   sing N N 112 
ASP   CA  C    sing N N 113 
ASP   CA  CB   sing N N 114 
ASP   CA  HA   sing N N 115 
ASP   C   O    doub N N 116 
ASP   C   OXT  sing N N 117 
ASP   CB  CG   sing N N 118 
ASP   CB  HB2  sing N N 119 
ASP   CB  HB3  sing N N 120 
ASP   CG  OD1  doub N N 121 
ASP   CG  OD2  sing N N 122 
ASP   OD2 HD2  sing N N 123 
ASP   OXT HXT  sing N N 124 
CYS   N   CA   sing N N 125 
CYS   N   H    sing N N 126 
CYS   N   H2   sing N N 127 
CYS   CA  C    sing N N 128 
CYS   CA  CB   sing N N 129 
CYS   CA  HA   sing N N 130 
CYS   C   O    doub N N 131 
CYS   C   OXT  sing N N 132 
CYS   CB  SG   sing N N 133 
CYS   CB  HB2  sing N N 134 
CYS   CB  HB3  sing N N 135 
CYS   SG  HG   sing N N 136 
CYS   OXT HXT  sing N N 137 
GLN   N   CA   sing N N 138 
GLN   N   H    sing N N 139 
GLN   N   H2   sing N N 140 
GLN   CA  C    sing N N 141 
GLN   CA  CB   sing N N 142 
GLN   CA  HA   sing N N 143 
GLN   C   O    doub N N 144 
GLN   C   OXT  sing N N 145 
GLN   CB  CG   sing N N 146 
GLN   CB  HB2  sing N N 147 
GLN   CB  HB3  sing N N 148 
GLN   CG  CD   sing N N 149 
GLN   CG  HG2  sing N N 150 
GLN   CG  HG3  sing N N 151 
GLN   CD  OE1  doub N N 152 
GLN   CD  NE2  sing N N 153 
GLN   NE2 HE21 sing N N 154 
GLN   NE2 HE22 sing N N 155 
GLN   OXT HXT  sing N N 156 
GLU   N   CA   sing N N 157 
GLU   N   H    sing N N 158 
GLU   N   H2   sing N N 159 
GLU   CA  C    sing N N 160 
GLU   CA  CB   sing N N 161 
GLU   CA  HA   sing N N 162 
GLU   C   O    doub N N 163 
GLU   C   OXT  sing N N 164 
GLU   CB  CG   sing N N 165 
GLU   CB  HB2  sing N N 166 
GLU   CB  HB3  sing N N 167 
GLU   CG  CD   sing N N 168 
GLU   CG  HG2  sing N N 169 
GLU   CG  HG3  sing N N 170 
GLU   CD  OE1  doub N N 171 
GLU   CD  OE2  sing N N 172 
GLU   OE2 HE2  sing N N 173 
GLU   OXT HXT  sing N N 174 
GLY   N   CA   sing N N 175 
GLY   N   H    sing N N 176 
GLY   N   H2   sing N N 177 
GLY   CA  C    sing N N 178 
GLY   CA  HA2  sing N N 179 
GLY   CA  HA3  sing N N 180 
GLY   C   O    doub N N 181 
GLY   C   OXT  sing N N 182 
GLY   OXT HXT  sing N N 183 
HIS   N   CA   sing N N 184 
HIS   N   H    sing N N 185 
HIS   N   H2   sing N N 186 
HIS   CA  C    sing N N 187 
HIS   CA  CB   sing N N 188 
HIS   CA  HA   sing N N 189 
HIS   C   O    doub N N 190 
HIS   C   OXT  sing N N 191 
HIS   CB  CG   sing N N 192 
HIS   CB  HB2  sing N N 193 
HIS   CB  HB3  sing N N 194 
HIS   CG  ND1  sing Y N 195 
HIS   CG  CD2  doub Y N 196 
HIS   ND1 CE1  doub Y N 197 
HIS   ND1 HD1  sing N N 198 
HIS   CD2 NE2  sing Y N 199 
HIS   CD2 HD2  sing N N 200 
HIS   CE1 NE2  sing Y N 201 
HIS   CE1 HE1  sing N N 202 
HIS   NE2 HE2  sing N N 203 
HIS   OXT HXT  sing N N 204 
HOH   O   H1   sing N N 205 
HOH   O   H2   sing N N 206 
ILE   N   CA   sing N N 207 
ILE   N   H    sing N N 208 
ILE   N   H2   sing N N 209 
ILE   CA  C    sing N N 210 
ILE   CA  CB   sing N N 211 
ILE   CA  HA   sing N N 212 
ILE   C   O    doub N N 213 
ILE   C   OXT  sing N N 214 
ILE   CB  CG1  sing N N 215 
ILE   CB  CG2  sing N N 216 
ILE   CB  HB   sing N N 217 
ILE   CG1 CD1  sing N N 218 
ILE   CG1 HG12 sing N N 219 
ILE   CG1 HG13 sing N N 220 
ILE   CG2 HG21 sing N N 221 
ILE   CG2 HG22 sing N N 222 
ILE   CG2 HG23 sing N N 223 
ILE   CD1 HD11 sing N N 224 
ILE   CD1 HD12 sing N N 225 
ILE   CD1 HD13 sing N N 226 
ILE   OXT HXT  sing N N 227 
LEU   N   CA   sing N N 228 
LEU   N   H    sing N N 229 
LEU   N   H2   sing N N 230 
LEU   CA  C    sing N N 231 
LEU   CA  CB   sing N N 232 
LEU   CA  HA   sing N N 233 
LEU   C   O    doub N N 234 
LEU   C   OXT  sing N N 235 
LEU   CB  CG   sing N N 236 
LEU   CB  HB2  sing N N 237 
LEU   CB  HB3  sing N N 238 
LEU   CG  CD1  sing N N 239 
LEU   CG  CD2  sing N N 240 
LEU   CG  HG   sing N N 241 
LEU   CD1 HD11 sing N N 242 
LEU   CD1 HD12 sing N N 243 
LEU   CD1 HD13 sing N N 244 
LEU   CD2 HD21 sing N N 245 
LEU   CD2 HD22 sing N N 246 
LEU   CD2 HD23 sing N N 247 
LEU   OXT HXT  sing N N 248 
LYS   N   CA   sing N N 249 
LYS   N   H    sing N N 250 
LYS   N   H2   sing N N 251 
LYS   CA  C    sing N N 252 
LYS   CA  CB   sing N N 253 
LYS   CA  HA   sing N N 254 
LYS   C   O    doub N N 255 
LYS   C   OXT  sing N N 256 
LYS   CB  CG   sing N N 257 
LYS   CB  HB2  sing N N 258 
LYS   CB  HB3  sing N N 259 
LYS   CG  CD   sing N N 260 
LYS   CG  HG2  sing N N 261 
LYS   CG  HG3  sing N N 262 
LYS   CD  CE   sing N N 263 
LYS   CD  HD2  sing N N 264 
LYS   CD  HD3  sing N N 265 
LYS   CE  NZ   sing N N 266 
LYS   CE  HE2  sing N N 267 
LYS   CE  HE3  sing N N 268 
LYS   NZ  HZ1  sing N N 269 
LYS   NZ  HZ2  sing N N 270 
LYS   NZ  HZ3  sing N N 271 
LYS   OXT HXT  sing N N 272 
MET   N   CA   sing N N 273 
MET   N   H    sing N N 274 
MET   N   H2   sing N N 275 
MET   CA  C    sing N N 276 
MET   CA  CB   sing N N 277 
MET   CA  HA   sing N N 278 
MET   C   O    doub N N 279 
MET   C   OXT  sing N N 280 
MET   CB  CG   sing N N 281 
MET   CB  HB2  sing N N 282 
MET   CB  HB3  sing N N 283 
MET   CG  SD   sing N N 284 
MET   CG  HG2  sing N N 285 
MET   CG  HG3  sing N N 286 
MET   SD  CE   sing N N 287 
MET   CE  HE1  sing N N 288 
MET   CE  HE2  sing N N 289 
MET   CE  HE3  sing N N 290 
MET   OXT HXT  sing N N 291 
PHE   N   CA   sing N N 292 
PHE   N   H    sing N N 293 
PHE   N   H2   sing N N 294 
PHE   CA  C    sing N N 295 
PHE   CA  CB   sing N N 296 
PHE   CA  HA   sing N N 297 
PHE   C   O    doub N N 298 
PHE   C   OXT  sing N N 299 
PHE   CB  CG   sing N N 300 
PHE   CB  HB2  sing N N 301 
PHE   CB  HB3  sing N N 302 
PHE   CG  CD1  doub Y N 303 
PHE   CG  CD2  sing Y N 304 
PHE   CD1 CE1  sing Y N 305 
PHE   CD1 HD1  sing N N 306 
PHE   CD2 CE2  doub Y N 307 
PHE   CD2 HD2  sing N N 308 
PHE   CE1 CZ   doub Y N 309 
PHE   CE1 HE1  sing N N 310 
PHE   CE2 CZ   sing Y N 311 
PHE   CE2 HE2  sing N N 312 
PHE   CZ  HZ   sing N N 313 
PHE   OXT HXT  sing N N 314 
PRO   N   CA   sing N N 315 
PRO   N   CD   sing N N 316 
PRO   N   H    sing N N 317 
PRO   CA  C    sing N N 318 
PRO   CA  CB   sing N N 319 
PRO   CA  HA   sing N N 320 
PRO   C   O    doub N N 321 
PRO   C   OXT  sing N N 322 
PRO   CB  CG   sing N N 323 
PRO   CB  HB2  sing N N 324 
PRO   CB  HB3  sing N N 325 
PRO   CG  CD   sing N N 326 
PRO   CG  HG2  sing N N 327 
PRO   CG  HG3  sing N N 328 
PRO   CD  HD2  sing N N 329 
PRO   CD  HD3  sing N N 330 
PRO   OXT HXT  sing N N 331 
SER   N   CA   sing N N 332 
SER   N   H    sing N N 333 
SER   N   H2   sing N N 334 
SER   CA  C    sing N N 335 
SER   CA  CB   sing N N 336 
SER   CA  HA   sing N N 337 
SER   C   O    doub N N 338 
SER   C   OXT  sing N N 339 
SER   CB  OG   sing N N 340 
SER   CB  HB2  sing N N 341 
SER   CB  HB3  sing N N 342 
SER   OG  HG   sing N N 343 
SER   OXT HXT  sing N N 344 
THR   N   CA   sing N N 345 
THR   N   H    sing N N 346 
THR   N   H2   sing N N 347 
THR   CA  C    sing N N 348 
THR   CA  CB   sing N N 349 
THR   CA  HA   sing N N 350 
THR   C   O    doub N N 351 
THR   C   OXT  sing N N 352 
THR   CB  OG1  sing N N 353 
THR   CB  CG2  sing N N 354 
THR   CB  HB   sing N N 355 
THR   OG1 HG1  sing N N 356 
THR   CG2 HG21 sing N N 357 
THR   CG2 HG22 sing N N 358 
THR   CG2 HG23 sing N N 359 
THR   OXT HXT  sing N N 360 
TRP   N   CA   sing N N 361 
TRP   N   H    sing N N 362 
TRP   N   H2   sing N N 363 
TRP   CA  C    sing N N 364 
TRP   CA  CB   sing N N 365 
TRP   CA  HA   sing N N 366 
TRP   C   O    doub N N 367 
TRP   C   OXT  sing N N 368 
TRP   CB  CG   sing N N 369 
TRP   CB  HB2  sing N N 370 
TRP   CB  HB3  sing N N 371 
TRP   CG  CD1  doub Y N 372 
TRP   CG  CD2  sing Y N 373 
TRP   CD1 NE1  sing Y N 374 
TRP   CD1 HD1  sing N N 375 
TRP   CD2 CE2  doub Y N 376 
TRP   CD2 CE3  sing Y N 377 
TRP   NE1 CE2  sing Y N 378 
TRP   NE1 HE1  sing N N 379 
TRP   CE2 CZ2  sing Y N 380 
TRP   CE3 CZ3  doub Y N 381 
TRP   CE3 HE3  sing N N 382 
TRP   CZ2 CH2  doub Y N 383 
TRP   CZ2 HZ2  sing N N 384 
TRP   CZ3 CH2  sing Y N 385 
TRP   CZ3 HZ3  sing N N 386 
TRP   CH2 HH2  sing N N 387 
TRP   OXT HXT  sing N N 388 
TYR   N   CA   sing N N 389 
TYR   N   H    sing N N 390 
TYR   N   H2   sing N N 391 
TYR   CA  C    sing N N 392 
TYR   CA  CB   sing N N 393 
TYR   CA  HA   sing N N 394 
TYR   C   O    doub N N 395 
TYR   C   OXT  sing N N 396 
TYR   CB  CG   sing N N 397 
TYR   CB  HB2  sing N N 398 
TYR   CB  HB3  sing N N 399 
TYR   CG  CD1  doub Y N 400 
TYR   CG  CD2  sing Y N 401 
TYR   CD1 CE1  sing Y N 402 
TYR   CD1 HD1  sing N N 403 
TYR   CD2 CE2  doub Y N 404 
TYR   CD2 HD2  sing N N 405 
TYR   CE1 CZ   doub Y N 406 
TYR   CE1 HE1  sing N N 407 
TYR   CE2 CZ   sing Y N 408 
TYR   CE2 HE2  sing N N 409 
TYR   CZ  OH   sing N N 410 
TYR   OH  HH   sing N N 411 
TYR   OXT HXT  sing N N 412 
VAL   N   CA   sing N N 413 
VAL   N   H    sing N N 414 
VAL   N   H2   sing N N 415 
VAL   CA  C    sing N N 416 
VAL   CA  CB   sing N N 417 
VAL   CA  HA   sing N N 418 
VAL   C   O    doub N N 419 
VAL   C   OXT  sing N N 420 
VAL   CB  CG1  sing N N 421 
VAL   CB  CG2  sing N N 422 
VAL   CB  HB   sing N N 423 
VAL   CG1 HG11 sing N N 424 
VAL   CG1 HG12 sing N N 425 
VAL   CG1 HG13 sing N N 426 
VAL   CG2 HG21 sing N N 427 
VAL   CG2 HG22 sing N N 428 
VAL   CG2 HG23 sing N N 429 
VAL   OXT HXT  sing N N 430 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'in house' 
# 
_atom_sites.entry_id                    9GC4 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.007434 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004518 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011870 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.012131 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LEU   A 1 10  ? 23.767 -32.356 17.432  1.00 51.90  ? 703  LEU   A N   1 
ATOM   2    C  CA  . LEU   A 1 10  ? 23.099 -31.483 18.393  1.00 52.18  ? 703  LEU   A CA  1 
ATOM   3    C  C   . LEU   A 1 10  ? 22.933 -32.279 19.731  1.00 52.64  ? 703  LEU   A C   1 
ATOM   4    O  O   . LEU   A 1 10  ? 23.597 -31.968 20.729  1.00 52.82  ? 703  LEU   A O   1 
ATOM   5    C  CB  . LEU   A 1 10  ? 21.748 -31.022 17.791  1.00 52.07  ? 703  LEU   A CB  1 
ATOM   6    C  CG  . LEU   A 1 10  ? 21.087 -29.774 18.353  1.00 53.02  ? 703  LEU   A CG  1 
ATOM   7    C  CD1 . LEU   A 1 10  ? 20.308 -29.122 17.326  1.00 53.10  ? 703  LEU   A CD1 1 
ATOM   8    C  CD2 . LEU   A 1 10  ? 20.099 -30.110 19.432  1.00 53.95  ? 703  LEU   A CD2 1 
ATOM   9    N  N   . LEU   A 1 11  ? 22.110 -33.347 19.721  1.00 52.24  ? 704  LEU   A N   1 
ATOM   10   C  CA  . LEU   A 1 11  ? 21.881 -34.181 20.896  1.00 51.92  ? 704  LEU   A CA  1 
ATOM   11   C  C   . LEU   A 1 11  ? 22.594 -35.512 20.723  1.00 50.84  ? 704  LEU   A C   1 
ATOM   12   O  O   . LEU   A 1 11  ? 22.271 -36.275 19.812  1.00 50.84  ? 704  LEU   A O   1 
ATOM   13   C  CB  . LEU   A 1 11  ? 20.371 -34.425 21.090  1.00 52.43  ? 704  LEU   A CB  1 
ATOM   14   C  CG  . LEU   A 1 11  ? 19.992 -35.374 22.235  1.00 54.17  ? 704  LEU   A CG  1 
ATOM   15   C  CD1 . LEU   A 1 11  ? 20.376 -34.787 23.606  1.00 54.26  ? 704  LEU   A CD1 1 
ATOM   16   C  CD2 . LEU   A 1 11  ? 18.514 -35.780 22.156  1.00 54.99  ? 704  LEU   A CD2 1 
ATOM   17   N  N   . ARG   A 1 12  ? 23.553 -35.797 21.602  1.00 49.82  ? 705  ARG   A N   1 
ATOM   18   C  CA  . ARG   A 1 12  ? 24.277 -37.051 21.552  1.00 49.45  ? 705  ARG   A CA  1 
ATOM   19   C  C   . ARG   A 1 12  ? 23.555 -38.108 22.374  1.00 48.97  ? 705  ARG   A C   1 
ATOM   20   O  O   . ARG   A 1 12  ? 23.341 -37.904 23.559  1.00 48.91  ? 705  ARG   A O   1 
ATOM   21   C  CB  . ARG   A 1 12  ? 25.686 -36.873 22.108  1.00 50.92  ? 705  ARG   A CB  1 
ATOM   22   C  CG  . ARG   A 1 12  ? 26.615 -36.113 21.208  1.00 55.18  ? 705  ARG   A CG  1 
ATOM   23   C  CD  . ARG   A 1 12  ? 27.805 -35.643 22.003  1.00 60.07  ? 705  ARG   A CD  1 
ATOM   24   N  NE  . ARG   A 1 12  ? 28.793 -34.976 21.157  1.00 64.70  ? 705  ARG   A NE  1 
ATOM   25   C  CZ  . ARG   A 1 12  ? 29.589 -33.991 21.566  1.00 68.36  ? 705  ARG   A CZ  1 
ATOM   26   N  NH1 . ARG   A 1 12  ? 30.457 -33.441 20.725  1.00 69.03  ? 705  ARG   A NH1 1 
ATOM   27   N  NH2 . ARG   A 1 12  ? 29.508 -33.533 22.812  1.00 67.98  ? 705  ARG   A NH2 1 
ATOM   28   N  N   . ILE   A 1 13  ? 23.186 -39.237 21.760  1.00 48.60  ? 706  ILE   A N   1 
ATOM   29   C  CA  . ILE   A 1 13  ? 22.555 -40.330 22.501  1.00 48.41  ? 706  ILE   A CA  1 
ATOM   30   C  C   . ILE   A 1 13  ? 23.703 -41.212 22.917  1.00 48.68  ? 706  ILE   A C   1 
ATOM   31   O  O   . ILE   A 1 13  ? 24.453 -41.679 22.063  1.00 48.93  ? 706  ILE   A O   1 
ATOM   32   C  CB  . ILE   A 1 13  ? 21.520 -41.124 21.690  1.00 48.36  ? 706  ILE   A CB  1 
ATOM   33   C  CG1 . ILE   A 1 13  ? 20.553 -40.205 20.938  1.00 49.03  ? 706  ILE   A CG1 1 
ATOM   34   C  CG2 . ILE   A 1 13  ? 20.808 -42.093 22.611  1.00 48.74  ? 706  ILE   A CG2 1 
ATOM   35   C  CD1 . ILE   A 1 13  ? 19.743 -39.277 21.819  1.00 50.03  ? 706  ILE   A CD1 1 
ATOM   36   N  N   . LEU   A 1 14  ? 23.891 -41.391 24.216  1.00 48.53  ? 707  LEU   A N   1 
ATOM   37   C  CA  . LEU   A 1 14  ? 25.034 -42.123 24.730  1.00 48.87  ? 707  LEU   A CA  1 
ATOM   38   C  C   . LEU   A 1 14  ? 24.743 -43.578 25.059  1.00 49.95  ? 707  LEU   A C   1 
ATOM   39   O  O   . LEU   A 1 14  ? 23.668 -43.913 25.566  1.00 50.36  ? 707  LEU   A O   1 
ATOM   40   C  CB  . LEU   A 1 14  ? 25.576 -41.411 25.976  1.00 48.54  ? 707  LEU   A CB  1 
ATOM   41   C  CG  . LEU   A 1 14  ? 26.662 -40.374 25.771  1.00 49.54  ? 707  LEU   A CG  1 
ATOM   42   C  CD1 . LEU   A 1 14  ? 26.209 -39.250 24.883  1.00 49.65  ? 707  LEU   A CD1 1 
ATOM   43   C  CD2 . LEU   A 1 14  ? 27.081 -39.802 27.087  1.00 50.47  ? 707  LEU   A CD2 1 
ATOM   44   N  N   . LYS   A 1 15  ? 25.717 -44.442 24.778  1.00 50.14  ? 708  LYS   A N   1 
ATOM   45   C  CA  . LYS   A 1 15  ? 25.667 -45.861 25.104  1.00 50.76  ? 708  LYS   A CA  1 
ATOM   46   C  C   . LYS   A 1 15  ? 26.335 -46.005 26.473  1.00 51.47  ? 708  LYS   A C   1 
ATOM   47   O  O   . LYS   A 1 15  ? 27.280 -45.266 26.764  1.00 51.58  ? 708  LYS   A O   1 
ATOM   48   C  CB  . LYS   A 1 15  ? 26.436 -46.682 24.060  1.00 52.66  ? 708  LYS   A CB  1 
ATOM   49   C  CG  . LYS   A 1 15  ? 25.812 -46.692 22.674  1.00 57.45  ? 708  LYS   A CG  1 
ATOM   50   C  CD  . LYS   A 1 15  ? 26.830 -47.112 21.598  1.00 62.74  ? 708  LYS   A CD  1 
ATOM   51   C  CE  . LYS   A 1 15  ? 26.208 -47.255 20.224  1.00 66.79  ? 708  LYS   A CE  1 
ATOM   52   N  NZ  . LYS   A 1 15  ? 25.491 -46.014 19.812  1.00 69.64  ? 708  LYS   A NZ  1 
ATOM   53   N  N   . GLU   A 1 16  ? 25.865 -46.948 27.324  1.00 51.63  ? 709  GLU   A N   1 
ATOM   54   C  CA  . GLU   A 1 16  ? 26.465 -47.131 28.645  1.00 52.13  ? 709  GLU   A CA  1 
ATOM   55   C  C   . GLU   A 1 16  ? 27.961 -47.453 28.593  1.00 52.62  ? 709  GLU   A C   1 
ATOM   56   O  O   . GLU   A 1 16  ? 28.668 -47.241 29.575  1.00 52.75  ? 709  GLU   A O   1 
ATOM   57   C  CB  . GLU   A 1 16  ? 25.736 -48.221 29.415  1.00 55.07  ? 709  GLU   A CB  1 
ATOM   58   C  CG  . GLU   A 1 16  ? 24.239 -48.013 29.542  1.00 60.78  ? 709  GLU   A CG  1 
ATOM   59   C  CD  . GLU   A 1 16  ? 23.607 -49.000 30.509  1.00 66.81  ? 709  GLU   A CD  1 
ATOM   60   O  OE1 . GLU   A 1 16  ? 22.884 -49.912 30.044  1.00 67.73  ? 709  GLU   A OE1 1 
ATOM   61   O  OE2 . GLU   A 1 16  ? 23.866 -48.879 31.730  1.00 68.41  ? 709  GLU   A OE2 1 
ATOM   62   N  N   . THR   A 1 17  ? 28.429 -47.969 27.444  1.00 53.05  ? 710  THR   A N   1 
ATOM   63   C  CA  . THR   A 1 17  ? 29.806 -48.336 27.140  1.00 53.93  ? 710  THR   A CA  1 
ATOM   64   C  C   . THR   A 1 17  ? 30.716 -47.101 26.931  1.00 54.69  ? 710  THR   A C   1 
ATOM   65   O  O   . THR   A 1 17  ? 31.927 -47.198 27.114  1.00 55.39  ? 710  THR   A O   1 
ATOM   66   C  CB  . THR   A 1 17  ? 29.794 -49.261 25.917  1.00 55.47  ? 710  THR   A CB  1 
ATOM   67   O  OG1 . THR   A 1 17  ? 29.169 -48.580 24.829  1.00 56.90  ? 710  THR   A OG1 1 
ATOM   68   C  CG2 . THR   A 1 17  ? 29.031 -50.554 26.171  1.00 55.91  ? 710  THR   A CG2 1 
ATOM   69   N  N   . GLU   A 1 18  ? 30.137 -45.944 26.562  1.00 54.33  ? 711  GLU   A N   1 
ATOM   70   C  CA  . GLU   A 1 18  ? 30.884 -44.711 26.325  1.00 54.28  ? 711  GLU   A CA  1 
ATOM   71   C  C   . GLU   A 1 18  ? 31.244 -43.954 27.590  1.00 54.56  ? 711  GLU   A C   1 
ATOM   72   O  O   . GLU   A 1 18  ? 32.076 -43.051 27.511  1.00 55.43  ? 711  GLU   A O   1 
ATOM   73   C  CB  . GLU   A 1 18  ? 30.078 -43.751 25.445  1.00 55.87  ? 711  GLU   A CB  1 
ATOM   74   C  CG  . GLU   A 1 18  ? 29.681 -44.290 24.089  1.00 59.38  ? 711  GLU   A CG  1 
ATOM   75   C  CD  . GLU   A 1 18  ? 28.929 -43.249 23.295  1.00 65.56  ? 711  GLU   A CD  1 
ATOM   76   O  OE1 . GLU   A 1 18  ? 29.293 -42.052 23.380  1.00 68.76  ? 711  GLU   A OE1 1 
ATOM   77   O  OE2 . GLU   A 1 18  ? 27.958 -43.625 22.604  1.00 66.29  ? 711  GLU   A OE2 1 
ATOM   78   N  N   . PHE   A 1 19  ? 30.577 -44.228 28.722  1.00 53.69  ? 712  PHE   A N   1 
ATOM   79   C  CA  . PHE   A 1 19  ? 30.852 -43.476 29.947  1.00 53.34  ? 712  PHE   A CA  1 
ATOM   80   C  C   . PHE   A 1 19  ? 30.854 -44.341 31.201  1.00 53.66  ? 712  PHE   A C   1 
ATOM   81   O  O   . PHE   A 1 19  ? 30.276 -45.427 31.218  1.00 53.89  ? 712  PHE   A O   1 
ATOM   82   C  CB  . PHE   A 1 19  ? 29.903 -42.276 30.093  1.00 52.76  ? 712  PHE   A CB  1 
ATOM   83   C  CG  . PHE   A 1 19  ? 28.457 -42.637 30.303  1.00 52.87  ? 712  PHE   A CG  1 
ATOM   84   C  CD1 . PHE   A 1 19  ? 27.644 -42.945 29.232  1.00 53.28  ? 712  PHE   A CD1 1 
ATOM   85   C  CD2 . PHE   A 1 19  ? 27.896 -42.615 31.568  1.00 53.42  ? 712  PHE   A CD2 1 
ATOM   86   C  CE1 . PHE   A 1 19  ? 26.314 -43.276 29.427  1.00 53.71  ? 712  PHE   A CE1 1 
ATOM   87   C  CE2 . PHE   A 1 19  ? 26.564 -42.947 31.758  1.00 53.83  ? 712  PHE   A CE2 1 
ATOM   88   C  CZ  . PHE   A 1 19  ? 25.781 -43.271 30.687  1.00 53.42  ? 712  PHE   A CZ  1 
ATOM   89   N  N   . LYS   A 1 20  ? 31.531 -43.862 32.248  1.00 53.46  ? 713  LYS   A N   1 
ATOM   90   C  CA  . LYS   A 1 20  ? 31.667 -44.573 33.502  1.00 53.88  ? 713  LYS   A CA  1 
ATOM   91   C  C   . LYS   A 1 20  ? 31.430 -43.609 34.632  1.00 54.51  ? 713  LYS   A C   1 
ATOM   92   O  O   . LYS   A 1 20  ? 32.126 -42.599 34.710  1.00 54.73  ? 713  LYS   A O   1 
ATOM   93   C  CB  . LYS   A 1 20  ? 33.101 -45.138 33.657  1.00 55.43  ? 713  LYS   A CB  1 
ATOM   94   C  CG  . LYS   A 1 20  ? 33.522 -46.170 32.608  1.00 59.21  ? 713  LYS   A CG  1 
ATOM   95   C  CD  . LYS   A 1 20  ? 34.756 -45.706 31.813  1.00 62.57  ? 713  LYS   A CD  1 
ATOM   96   C  CE  . LYS   A 1 20  ? 34.474 -45.524 30.334  1.00 64.79  ? 713  LYS   A CE  1 
ATOM   97   N  NZ  . LYS   A 1 20  ? 35.242 -44.390 29.765  1.00 65.05  ? 713  LYS   A NZ  1 
ATOM   98   N  N   . LYS   A 1 21  ? 30.491 -43.927 35.534  1.00 54.48  ? 714  LYS   A N   1 
ATOM   99   C  CA  . LYS   A 1 21  ? 30.272 -43.125 36.729  1.00 54.99  ? 714  LYS   A CA  1 
ATOM   100  C  C   . LYS   A 1 21  ? 31.372 -43.545 37.707  1.00 56.29  ? 714  LYS   A C   1 
ATOM   101  O  O   . LYS   A 1 21  ? 31.577 -44.745 37.920  1.00 56.69  ? 714  LYS   A O   1 
ATOM   102  C  CB  . LYS   A 1 21  ? 28.906 -43.406 37.350  1.00 55.84  ? 714  LYS   A CB  1 
ATOM   103  C  CG  . LYS   A 1 21  ? 27.804 -43.522 36.323  1.00 58.58  ? 714  LYS   A CG  1 
ATOM   104  C  CD  . LYS   A 1 21  ? 26.479 -43.049 36.828  1.00 61.35  ? 714  LYS   A CD  1 
ATOM   105  C  CE  . LYS   A 1 21  ? 25.533 -44.171 37.179  1.00 63.79  ? 714  LYS   A CE  1 
ATOM   106  N  NZ  . LYS   A 1 21  ? 24.936 -44.790 35.976  1.00 65.98  ? 714  LYS   A NZ  1 
ATOM   107  N  N   . ILE   A 1 22  ? 32.099 -42.580 38.283  1.00 56.79  ? 715  ILE   A N   1 
ATOM   108  C  CA  . ILE   A 1 22  ? 33.199 -42.902 39.187  1.00 57.55  ? 715  ILE   A CA  1 
ATOM   109  C  C   . ILE   A 1 22  ? 32.861 -42.656 40.670  1.00 58.02  ? 715  ILE   A C   1 
ATOM   110  O  O   . ILE   A 1 22  ? 32.940 -43.590 41.461  1.00 58.34  ? 715  ILE   A O   1 
ATOM   111  C  CB  . ILE   A 1 22  ? 34.471 -42.167 38.721  1.00 58.17  ? 715  ILE   A CB  1 
ATOM   112  C  CG1 . ILE   A 1 22  ? 34.918 -42.721 37.354  1.00 59.09  ? 715  ILE   A CG1 1 
ATOM   113  C  CG2 . ILE   A 1 22  ? 35.587 -42.269 39.756  1.00 58.74  ? 715  ILE   A CG2 1 
ATOM   114  C  CD1 . ILE   A 1 22  ? 35.871 -41.840 36.638  1.00 60.84  ? 715  ILE   A CD1 1 
ATOM   115  N  N   . LYS   A 1 23  ? 32.475 -41.433 41.049  1.00 57.94  ? 716  LYS   A N   1 
ATOM   116  C  CA  . LYS   A 1 23  ? 32.160 -41.122 42.443  1.00 58.18  ? 716  LYS   A CA  1 
ATOM   117  C  C   . LYS   A 1 23  ? 30.811 -40.419 42.567  1.00 58.01  ? 716  LYS   A C   1 
ATOM   118  O  O   . LYS   A 1 23  ? 30.376 -39.763 41.632  1.00 58.04  ? 716  LYS   A O   1 
ATOM   119  C  CB  . LYS   A 1 23  ? 33.257 -40.216 43.028  1.00 60.63  ? 716  LYS   A CB  1 
ATOM   120  C  CG  . LYS   A 1 23  ? 33.443 -40.356 44.543  1.00 65.71  ? 716  LYS   A CG  1 
ATOM   121  C  CD  . LYS   A 1 23  ? 34.661 -39.562 45.048  1.00 71.11  ? 716  LYS   A CD  1 
ATOM   122  C  CE  . LYS   A 1 23  ? 35.978 -39.931 44.389  1.00 75.20  ? 716  LYS   A CE  1 
ATOM   123  N  NZ  . LYS   A 1 23  ? 36.371 -38.973 43.307  1.00 77.36  ? 716  LYS   A NZ  1 
ATOM   124  N  N   . VAL   A 1 24  ? 30.165 -40.513 43.733  1.00 57.70  ? 717  VAL   A N   1 
ATOM   125  C  CA  . VAL   A 1 24  ? 28.892 -39.833 43.955  1.00 57.46  ? 717  VAL   A CA  1 
ATOM   126  C  C   . VAL   A 1 24  ? 29.151 -38.426 44.456  1.00 57.82  ? 717  VAL   A C   1 
ATOM   127  O  O   . VAL   A 1 24  ? 29.876 -38.244 45.437  1.00 58.29  ? 717  VAL   A O   1 
ATOM   128  C  CB  . VAL   A 1 24  ? 27.959 -40.616 44.902  1.00 57.35  ? 717  VAL   A CB  1 
ATOM   129  C  CG1 . VAL   A 1 24  ? 26.641 -39.879 45.102  1.00 57.65  ? 717  VAL   A CG1 1 
ATOM   130  C  CG2 . VAL   A 1 24  ? 27.711 -42.017 44.370  1.00 57.61  ? 717  VAL   A CG2 1 
ATOM   131  N  N   . LEU   A 1 25  ? 28.587 -37.426 43.772  1.00 57.47  ? 718  LEU   A N   1 
ATOM   132  C  CA  . LEU   A 1 25  ? 28.738 -36.045 44.201  1.00 57.62  ? 718  LEU   A CA  1 
ATOM   133  C  C   . LEU   A 1 25  ? 27.636 -35.626 45.174  1.00 58.07  ? 718  LEU   A C   1 
ATOM   134  O  O   . LEU   A 1 25  ? 27.889 -34.844 46.087  1.00 58.39  ? 718  LEU   A O   1 
ATOM   135  C  CB  . LEU   A 1 25  ? 28.775 -35.107 42.998  1.00 57.68  ? 718  LEU   A CB  1 
ATOM   136  C  CG  . LEU   A 1 25  ? 29.891 -35.362 42.009  1.00 59.11  ? 718  LEU   A CG  1 
ATOM   137  C  CD1 . LEU   A 1 25  ? 29.805 -34.393 40.857  1.00 59.55  ? 718  LEU   A CD1 1 
ATOM   138  C  CD2 . LEU   A 1 25  ? 31.264 -35.282 42.684  1.00 59.78  ? 718  LEU   A CD2 1 
ATOM   139  N  N   . GLY   A 1 26  ? 26.429 -36.131 44.964  1.00 57.93  ? 719  GLY   A N   1 
ATOM   140  C  CA  . GLY   A 1 26  ? 25.311 -35.798 45.822  1.00 58.55  ? 719  GLY   A CA  1 
ATOM   141  C  C   . GLY   A 1 26  ? 24.006 -36.385 45.353  1.00 59.41  ? 719  GLY   A C   1 
ATOM   142  O  O   . GLY   A 1 26  ? 23.880 -36.803 44.204  1.00 59.02  ? 719  GLY   A O   1 
ATOM   143  N  N   . SER   A 1 27  ? 23.036 -36.434 46.261  1.00 60.62  ? 720  SER   A N   1 
ATOM   144  C  CA  . SER   A 1 27  ? 21.718 -36.969 45.961  1.00 62.22  ? 720  SER   A CA  1 
ATOM   145  C  C   . SER   A 1 27  ? 20.627 -35.979 46.363  1.00 63.99  ? 720  SER   A C   1 
ATOM   146  O  O   . SER   A 1 27  ? 20.439 -35.687 47.541  1.00 64.09  ? 720  SER   A O   1 
ATOM   147  C  CB  . SER   A 1 27  ? 21.509 -38.308 46.653  1.00 63.13  ? 720  SER   A CB  1 
ATOM   148  O  OG  . SER   A 1 27  ? 22.538 -39.218 46.302  1.00 65.31  ? 720  SER   A OG  1 
ATOM   149  N  N   . GLY   A 1 28  ? 19.940 -35.440 45.368  1.00 65.00  ? 721  GLY   A N   1 
ATOM   150  C  CA  . GLY   A 1 28  ? 18.849 -34.508 45.607  1.00 65.83  ? 721  GLY   A CA  1 
ATOM   151  C  C   . GLY   A 1 28  ? 17.533 -35.245 45.727  1.00 66.38  ? 721  GLY   A C   1 
ATOM   152  O  O   . GLY   A 1 28  ? 17.502 -36.419 46.111  1.00 66.78  ? 721  GLY   A O   1 
ATOM   153  N  N   . ALA   A 1 29  ? 16.438 -34.563 45.408  1.00 66.26  ? 722  ALA   A N   1 
ATOM   154  C  CA  . ALA   A 1 29  ? 15.117 -35.184 45.467  1.00 66.75  ? 722  ALA   A CA  1 
ATOM   155  C  C   . ALA   A 1 29  ? 14.803 -35.892 44.148  1.00 66.69  ? 722  ALA   A C   1 
ATOM   156  O  O   . ALA   A 1 29  ? 14.245 -36.998 44.143  1.00 66.69  ? 722  ALA   A O   1 
ATOM   157  C  CB  . ALA   A 1 29  ? 14.062 -34.127 45.761  1.00 67.16  ? 722  ALA   A CB  1 
ATOM   158  N  N   . PHE   A 1 30  ? 15.202 -35.254 43.034  1.00 66.32  ? 723  PHE   A N   1 
ATOM   159  C  CA  . PHE   A 1 30  ? 14.958 -35.729 41.682  1.00 66.73  ? 723  PHE   A CA  1 
ATOM   160  C  C   . PHE   A 1 30  ? 15.937 -36.799 41.179  1.00 65.57  ? 723  PHE   A C   1 
ATOM   161  O  O   . PHE   A 1 30  ? 15.676 -37.397 40.136  1.00 65.95  ? 723  PHE   A O   1 
ATOM   162  C  CB  . PHE   A 1 30  ? 14.900 -34.547 40.702  1.00 67.57  ? 723  PHE   A CB  1 
ATOM   163  C  CG  . PHE   A 1 30  ? 13.951 -33.448 41.148  1.00 69.02  ? 723  PHE   A CG  1 
ATOM   164  C  CD1 . PHE   A 1 30  ? 12.653 -33.745 41.553  1.00 70.08  ? 723  PHE   A CD1 1 
ATOM   165  C  CD2 . PHE   A 1 30  ? 14.360 -32.128 41.183  1.00 69.96  ? 723  PHE   A CD2 1 
ATOM   166  C  CE1 . PHE   A 1 30  ? 11.788 -32.738 41.977  1.00 70.86  ? 723  PHE   A CE1 1 
ATOM   167  C  CE2 . PHE   A 1 30  ? 13.489 -31.125 41.606  1.00 70.77  ? 723  PHE   A CE2 1 
ATOM   168  C  CZ  . PHE   A 1 30  ? 12.213 -31.438 42.003  1.00 70.57  ? 723  PHE   A CZ  1 
ATOM   169  N  N   . GLY   A 1 31  ? 17.024 -37.048 41.907  1.00 63.80  ? 724  GLY   A N   1 
ATOM   170  C  CA  . GLY   A 1 31  ? 17.979 -38.074 41.509  1.00 62.23  ? 724  GLY   A CA  1 
ATOM   171  C  C   . GLY   A 1 31  ? 19.349 -37.961 42.135  1.00 59.99  ? 724  GLY   A C   1 
ATOM   172  O  O   . GLY   A 1 31  ? 19.536 -37.227 43.104  1.00 59.52  ? 724  GLY   A O   1 
ATOM   173  N  N   . THR   A 1 32  ? 20.330 -38.675 41.560  1.00 58.37  ? 725  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 32  ? 21.710 -38.667 42.055  1.00 57.06  ? 725  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 32  ? 22.673 -38.148 40.988  1.00 55.19  ? 725  THR   A C   1 
ATOM   176  O  O   . THR   A 1 32  ? 22.586 -38.573 39.837  1.00 54.85  ? 725  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 32  ? 22.147 -40.086 42.422  1.00 58.44  ? 725  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 32  ? 21.148 -40.712 43.236  1.00 60.13  ? 725  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 32  ? 23.518 -40.127 43.085  1.00 58.46  ? 725  THR   A CG2 1 
ATOM   180  N  N   . VAL   A 1 33  ? 23.612 -37.262 41.368  1.00 53.67  ? 726  VAL   A N   1 
ATOM   181  C  CA  . VAL   A 1 33  ? 24.595 -36.772 40.409  1.00 52.62  ? 726  VAL   A CA  1 
ATOM   182  C  C   . VAL   A 1 33  ? 25.964 -37.407 40.758  1.00 52.30  ? 726  VAL   A C   1 
ATOM   183  O  O   . VAL   A 1 33  ? 26.341 -37.512 41.926  1.00 52.17  ? 726  VAL   A O   1 
ATOM   184  C  CB  . VAL   A 1 33  ? 24.622 -35.226 40.121  1.00 51.89  ? 726  VAL   A CB  1 
ATOM   185  C  CG1 . VAL   A 1 33  ? 23.401 -34.508 40.674  1.00 51.87  ? 726  VAL   A CG1 1 
ATOM   186  C  CG2 . VAL   A 1 33  ? 25.916 -34.552 40.553  1.00 51.92  ? 726  VAL   A CG2 1 
ATOM   187  N  N   . TYR   A 1 34  ? 26.654 -37.898 39.716  1.00 51.77  ? 727  TYR   A N   1 
ATOM   188  C  CA  . TYR   A 1 34  ? 27.945 -38.562 39.802  1.00 51.83  ? 727  TYR   A CA  1 
ATOM   189  C  C   . TYR   A 1 34  ? 29.016 -37.808 39.020  1.00 51.76  ? 727  TYR   A C   1 
ATOM   190  O  O   . TYR   A 1 34  ? 28.750 -37.218 37.992  1.00 51.21  ? 727  TYR   A O   1 
ATOM   191  C  CB  . TYR   A 1 34  ? 27.874 -39.979 39.185  1.00 51.76  ? 727  TYR   A CB  1 
ATOM   192  C  CG  . TYR   A 1 34  ? 26.838 -40.908 39.769  1.00 52.53  ? 727  TYR   A CG  1 
ATOM   193  C  CD1 . TYR   A 1 34  ? 25.505 -40.814 39.397  1.00 53.39  ? 727  TYR   A CD1 1 
ATOM   194  C  CD2 . TYR   A 1 34  ? 27.204 -41.945 40.612  1.00 53.68  ? 727  TYR   A CD2 1 
ATOM   195  C  CE1 . TYR   A 1 34  ? 24.552 -41.689 39.899  1.00 54.62  ? 727  TYR   A CE1 1 
ATOM   196  C  CE2 . TYR   A 1 34  ? 26.262 -42.833 41.117  1.00 54.73  ? 727  TYR   A CE2 1 
ATOM   197  C  CZ  . TYR   A 1 34  ? 24.936 -42.705 40.754  1.00 55.79  ? 727  TYR   A CZ  1 
ATOM   198  O  OH  . TYR   A 1 34  ? 23.999 -43.582 41.248  1.00 57.47  ? 727  TYR   A OH  1 
ATOM   199  N  N   . LYS   A 1 35  ? 30.240 -37.904 39.484  1.00 52.31  ? 728  LYS   A N   1 
ATOM   200  C  CA  . LYS   A 1 35  ? 31.419 -37.408 38.804  1.00 53.35  ? 728  LYS   A CA  1 
ATOM   201  C  C   . LYS   A 1 35  ? 31.813 -38.589 37.906  1.00 53.80  ? 728  LYS   A C   1 
ATOM   202  O  O   . LYS   A 1 35  ? 31.988 -39.696 38.417  1.00 54.44  ? 728  LYS   A O   1 
ATOM   203  C  CB  . LYS   A 1 35  ? 32.514 -37.158 39.856  1.00 55.96  ? 728  LYS   A CB  1 
ATOM   204  C  CG  . LYS   A 1 35  ? 33.923 -37.007 39.321  1.00 62.16  ? 728  LYS   A CG  1 
ATOM   205  C  CD  . LYS   A 1 35  ? 34.882 -36.785 40.481  1.00 68.70  ? 728  LYS   A CD  1 
ATOM   206  C  CE  . LYS   A 1 35  ? 36.310 -36.558 40.054  1.00 73.99  ? 728  LYS   A CE  1 
ATOM   207  N  NZ  . LYS   A 1 35  ? 37.261 -36.949 41.136  1.00 76.59  ? 728  LYS   A NZ  1 
ATOM   208  N  N   . GLY   A 1 36  ? 31.887 -38.385 36.599  1.00 53.42  ? 729  GLY   A N   1 
ATOM   209  C  CA  . GLY   A 1 36  ? 32.207 -39.474 35.684  1.00 53.98  ? 729  GLY   A CA  1 
ATOM   210  C  C   . GLY   A 1 36  ? 33.230 -39.168 34.613  1.00 54.80  ? 729  GLY   A C   1 
ATOM   211  O  O   . GLY   A 1 36  ? 33.837 -38.099 34.601  1.00 55.21  ? 729  GLY   A O   1 
ATOM   212  N  N   . LEU   A 1 37  ? 33.426 -40.121 33.697  1.00 54.97  ? 730  LEU   A N   1 
ATOM   213  C  CA  . LEU   A 1 37  ? 34.365 -39.995 32.583  1.00 55.34  ? 730  LEU   A CA  1 
ATOM   214  C  C   . LEU   A 1 37  ? 33.679 -40.411 31.294  1.00 55.39  ? 730  LEU   A C   1 
ATOM   215  O  O   . LEU   A 1 37  ? 32.949 -41.391 31.294  1.00 55.35  ? 730  LEU   A O   1 
ATOM   216  C  CB  . LEU   A 1 37  ? 35.586 -40.882 32.833  1.00 55.70  ? 730  LEU   A CB  1 
ATOM   217  C  CG  . LEU   A 1 37  ? 36.934 -40.191 32.690  1.00 57.37  ? 730  LEU   A CG  1 
ATOM   218  C  CD1 . LEU   A 1 37  ? 37.083 -39.074 33.698  1.00 57.85  ? 730  LEU   A CD1 1 
ATOM   219  C  CD2 . LEU   A 1 37  ? 38.057 -41.180 32.860  1.00 58.08  ? 730  LEU   A CD2 1 
ATOM   220  N  N   . TRP   A 1 38  ? 33.910 -39.691 30.201  1.00 55.70  ? 731  TRP   A N   1 
ATOM   221  C  CA  . TRP   A 1 38  ? 33.250 -39.998 28.942  1.00 56.67  ? 731  TRP   A CA  1 
ATOM   222  C  C   . TRP   A 1 38  ? 34.177 -40.005 27.736  1.00 58.26  ? 731  TRP   A C   1 
ATOM   223  O  O   . TRP   A 1 38  ? 34.822 -39.007 27.452  1.00 58.55  ? 731  TRP   A O   1 
ATOM   224  C  CB  . TRP   A 1 38  ? 32.080 -39.035 28.743  1.00 56.29  ? 731  TRP   A CB  1 
ATOM   225  C  CG  . TRP   A 1 38  ? 31.434 -39.091 27.395  1.00 56.40  ? 731  TRP   A CG  1 
ATOM   226  C  CD1 . TRP   A 1 38  ? 30.920 -40.189 26.771  1.00 57.06  ? 731  TRP   A CD1 1 
ATOM   227  C  CD2 . TRP   A 1 38  ? 31.144 -37.974 26.550  1.00 56.58  ? 731  TRP   A CD2 1 
ATOM   228  N  NE1 . TRP   A 1 38  ? 30.374 -39.832 25.563  1.00 57.52  ? 731  TRP   A NE1 1 
ATOM   229  C  CE2 . TRP   A 1 38  ? 30.487 -38.472 25.408  1.00 57.43  ? 731  TRP   A CE2 1 
ATOM   230  C  CE3 . TRP   A 1 38  ? 31.380 -36.597 26.646  1.00 57.08  ? 731  TRP   A CE3 1 
ATOM   231  C  CZ2 . TRP   A 1 38  ? 30.070 -37.643 24.369  1.00 58.10  ? 731  TRP   A CZ2 1 
ATOM   232  C  CZ3 . TRP   A 1 38  ? 30.988 -35.784 25.605  1.00 58.13  ? 731  TRP   A CZ3 1 
ATOM   233  C  CH2 . TRP   A 1 38  ? 30.343 -36.307 24.483  1.00 58.26  ? 731  TRP   A CH2 1 
ATOM   234  N  N   . ILE   A 1 39  ? 34.195 -41.119 26.998  1.00 59.27  ? 732  ILE   A N   1 
ATOM   235  C  CA  . ILE   A 1 39  ? 34.972 -41.269 25.770  1.00 60.87  ? 732  ILE   A CA  1 
ATOM   236  C  C   . ILE   A 1 39  ? 33.991 -41.347 24.618  1.00 62.43  ? 732  ILE   A C   1 
ATOM   237  O  O   . ILE   A 1 39  ? 33.362 -42.384 24.412  1.00 62.17  ? 732  ILE   A O   1 
ATOM   238  C  CB  . ILE   A 1 39  ? 35.843 -42.539 25.814  1.00 61.52  ? 732  ILE   A CB  1 
ATOM   239  C  CG1 . ILE   A 1 39  ? 36.711 -42.561 27.082  1.00 62.88  ? 732  ILE   A CG1 1 
ATOM   240  C  CG2 . ILE   A 1 39  ? 36.678 -42.682 24.538  1.00 61.69  ? 732  ILE   A CG2 1 
ATOM   241  C  CD1 . ILE   A 1 39  ? 37.384 -43.867 27.320  1.00 64.22  ? 732  ILE   A CD1 1 
ATOM   242  N  N   . PRO   A 1 40  ? 33.820 -40.254 23.867  1.00 63.96  ? 733  PRO   A N   1 
ATOM   243  C  CA  . PRO   A 1 40  ? 32.851 -40.279 22.757  1.00 65.52  ? 733  PRO   A CA  1 
ATOM   244  C  C   . PRO   A 1 40  ? 33.120 -41.372 21.722  1.00 68.24  ? 733  PRO   A C   1 
ATOM   245  O  O   . PRO   A 1 40  ? 34.227 -41.905 21.664  1.00 68.42  ? 733  PRO   A O   1 
ATOM   246  C  CB  . PRO   A 1 40  ? 32.932 -38.865 22.173  1.00 65.59  ? 733  PRO   A CB  1 
ATOM   247  C  CG  . PRO   A 1 40  ? 33.559 -38.031 23.247  1.00 65.47  ? 733  PRO   A CG  1 
ATOM   248  C  CD  . PRO   A 1 40  ? 34.474 -38.939 24.004  1.00 63.52  ? 733  PRO   A CD  1 
ATOM   249  N  N   . GLU   A 1 41  ? 32.086 -41.735 20.935  1.00 70.15  ? 734  GLU   A N   1 
ATOM   250  C  CA  . GLU   A 1 41  ? 32.148 -42.800 19.933  1.00 72.28  ? 734  GLU   A CA  1 
ATOM   251  C  C   . GLU   A 1 41  ? 33.386 -42.718 19.009  1.00 73.63  ? 734  GLU   A C   1 
ATOM   252  O  O   . GLU   A 1 41  ? 34.209 -43.643 19.014  1.00 74.18  ? 734  GLU   A O   1 
ATOM   253  C  CB  . GLU   A 1 41  ? 30.838 -42.888 19.119  1.00 75.52  ? 734  GLU   A CB  1 
ATOM   254  C  CG  . GLU   A 1 41  ? 29.806 -43.833 19.715  1.00 82.20  ? 734  GLU   A CG  1 
ATOM   255  C  CD  . GLU   A 1 41  ? 29.955 -45.308 19.378  1.00 90.30  ? 734  GLU   A CD  1 
ATOM   256  O  OE1 . GLU   A 1 41  ? 30.854 -45.971 19.947  1.00 91.75  ? 734  GLU   A OE1 1 
ATOM   257  O  OE2 . GLU   A 1 41  ? 29.148 -45.806 18.560  1.00 92.88  ? 734  GLU   A OE2 1 
ATOM   258  N  N   . GLY   A 1 42  ? 33.523 -41.630 18.253  1.00 73.74  ? 735  GLY   A N   1 
ATOM   259  C  CA  . GLY   A 1 42  ? 34.664 -41.474 17.359  1.00 74.28  ? 735  GLY   A CA  1 
ATOM   260  C  C   . GLY   A 1 42  ? 35.956 -41.218 18.111  1.00 74.50  ? 735  GLY   A C   1 
ATOM   261  O  O   . GLY   A 1 42  ? 36.943 -41.946 17.951  1.00 74.99  ? 735  GLY   A O   1 
ATOM   262  N  N   . GLU   A 1 43  ? 35.922 -40.212 18.989  1.00 73.78  ? 736  GLU   A N   1 
ATOM   263  C  CA  . GLU   A 1 43  ? 37.037 -39.756 19.808  1.00 73.61  ? 736  GLU   A CA  1 
ATOM   264  C  C   . GLU   A 1 43  ? 37.812 -40.849 20.555  1.00 73.09  ? 736  GLU   A C   1 
ATOM   265  O  O   . GLU   A 1 43  ? 37.321 -41.955 20.784  1.00 73.29  ? 736  GLU   A O   1 
ATOM   266  C  CB  . GLU   A 1 43  ? 36.556 -38.684 20.803  1.00 76.07  ? 736  GLU   A CB  1 
ATOM   267  C  CG  . GLU   A 1 43  ? 36.420 -37.298 20.202  1.00 80.97  ? 736  GLU   A CG  1 
ATOM   268  C  CD  . GLU   A 1 43  ? 35.063 -36.978 19.609  1.00 87.73  ? 736  GLU   A CD  1 
ATOM   269  O  OE1 . GLU   A 1 43  ? 34.728 -35.776 19.555  1.00 89.18  ? 736  GLU   A OE1 1 
ATOM   270  O  OE2 . GLU   A 1 43  ? 34.333 -37.911 19.202  1.00 90.29  ? 736  GLU   A OE2 1 
ATOM   271  N  N   . LYS   A 1 44  ? 39.051 -40.519 20.906  1.00 72.43  ? 737  LYS   A N   1 
ATOM   272  C  CA  . LYS   A 1 44  ? 39.962 -41.368 21.656  1.00 72.29  ? 737  LYS   A CA  1 
ATOM   273  C  C   . LYS   A 1 44  ? 40.478 -40.574 22.869  1.00 71.49  ? 737  LYS   A C   1 
ATOM   274  O  O   . LYS   A 1 44  ? 41.668 -40.640 23.185  1.00 71.92  ? 737  LYS   A O   1 
ATOM   275  C  CB  . LYS   A 1 44  ? 41.136 -41.797 20.753  1.00 74.47  ? 737  LYS   A CB  1 
ATOM   276  C  CG  . LYS   A 1 44  ? 40.717 -42.641 19.551  1.00 78.51  ? 737  LYS   A CG  1 
ATOM   277  C  CD  . LYS   A 1 44  ? 41.880 -42.893 18.611  1.00 82.81  ? 737  LYS   A CD  1 
ATOM   278  C  CE  . LYS   A 1 44  ? 41.679 -44.150 17.810  1.00 87.00  ? 737  LYS   A CE  1 
ATOM   279  N  NZ  . LYS   A 1 44  ? 41.635 -45.353 18.686  1.00 89.49  ? 737  LYS   A NZ  1 
ATOM   280  N  N   . VAL   A 1 45  ? 39.587 -39.799 23.528  1.00 70.18  ? 738  VAL   A N   1 
ATOM   281  C  CA  . VAL   A 1 45  ? 39.909 -38.965 24.694  1.00 69.30  ? 738  VAL   A CA  1 
ATOM   282  C  C   . VAL   A 1 45  ? 38.917 -39.191 25.840  1.00 67.94  ? 738  VAL   A C   1 
ATOM   283  O  O   . VAL   A 1 45  ? 37.791 -39.621 25.601  1.00 68.07  ? 738  VAL   A O   1 
ATOM   284  C  CB  . VAL   A 1 45  ? 40.006 -37.457 24.324  1.00 69.93  ? 738  VAL   A CB  1 
ATOM   285  C  CG1 . VAL   A 1 45  ? 41.268 -37.168 23.521  1.00 70.42  ? 738  VAL   A CG1 1 
ATOM   286  C  CG2 . VAL   A 1 45  ? 38.760 -36.985 23.577  1.00 70.31  ? 738  VAL   A CG2 1 
ATOM   287  N  N   . LYS   A 1 46  ? 39.323 -38.882 27.080  1.00 66.51  ? 739  LYS   A N   1 
ATOM   288  C  CA  . LYS   A 1 46  ? 38.447 -39.055 28.243  1.00 65.42  ? 739  LYS   A CA  1 
ATOM   289  C  C   . LYS   A 1 46  ? 38.016 -37.709 28.837  1.00 63.41  ? 739  LYS   A C   1 
ATOM   290  O  O   . LYS   A 1 46  ? 38.751 -37.109 29.617  1.00 63.84  ? 739  LYS   A O   1 
ATOM   291  C  CB  . LYS   A 1 46  ? 39.109 -39.943 29.315  1.00 67.88  ? 739  LYS   A CB  1 
ATOM   292  C  CG  . LYS   A 1 46  ? 39.686 -41.251 28.762  1.00 72.66  ? 739  LYS   A CG  1 
ATOM   293  C  CD  . LYS   A 1 46  ? 39.750 -42.348 29.823  1.00 77.76  ? 739  LYS   A CD  1 
ATOM   294  C  CE  . LYS   A 1 46  ? 40.854 -43.356 29.590  1.00 82.35  ? 739  LYS   A CE  1 
ATOM   295  N  NZ  . LYS   A 1 46  ? 40.727 -44.036 28.273  1.00 85.25  ? 739  LYS   A NZ  1 
ATOM   296  N  N   . ILE   A 1 47  ? 36.819 -37.247 28.475  1.00 61.12  ? 740  ILE   A N   1 
ATOM   297  C  CA  . ILE   A 1 47  ? 36.248 -35.991 28.958  1.00 59.37  ? 740  ILE   A CA  1 
ATOM   298  C  C   . ILE   A 1 47  ? 35.649 -36.157 30.357  1.00 57.80  ? 740  ILE   A C   1 
ATOM   299  O  O   . ILE   A 1 47  ? 34.751 -36.974 30.537  1.00 57.62  ? 740  ILE   A O   1 
ATOM   300  C  CB  . ILE   A 1 47  ? 35.151 -35.517 27.973  1.00 59.47  ? 740  ILE   A CB  1 
ATOM   301  C  CG1 . ILE   A 1 47  ? 35.683 -35.425 26.536  1.00 60.24  ? 740  ILE   A CG1 1 
ATOM   302  C  CG2 . ILE   A 1 47  ? 34.524 -34.206 28.431  1.00 59.64  ? 740  ILE   A CG2 1 
ATOM   303  C  CD1 . ILE   A 1 47  ? 34.619 -35.293 25.523  1.00 61.20  ? 740  ILE   A CD1 1 
ATOM   304  N  N   . PRO   A 1 48  ? 36.087 -35.360 31.350  1.00 56.45  ? 741  PRO   A N   1 
ATOM   305  C  CA  . PRO   A 1 48  ? 35.476 -35.461 32.689  1.00 55.17  ? 741  PRO   A CA  1 
ATOM   306  C  C   . PRO   A 1 48  ? 34.094 -34.803 32.738  1.00 53.47  ? 741  PRO   A C   1 
ATOM   307  O  O   . PRO   A 1 48  ? 33.974 -33.590 32.547  1.00 53.61  ? 741  PRO   A O   1 
ATOM   308  C  CB  . PRO   A 1 48  ? 36.486 -34.773 33.612  1.00 55.99  ? 741  PRO   A CB  1 
ATOM   309  C  CG  . PRO   A 1 48  ? 37.360 -33.963 32.725  1.00 56.74  ? 741  PRO   A CG  1 
ATOM   310  C  CD  . PRO   A 1 48  ? 37.129 -34.315 31.288  1.00 55.66  ? 741  PRO   A CD  1 
ATOM   311  N  N   . VAL   A 1 49  ? 33.047 -35.622 32.953  1.00 51.50  ? 742  VAL   A N   1 
ATOM   312  C  CA  . VAL   A 1 49  ? 31.656 -35.164 32.966  1.00 49.47  ? 742  VAL   A CA  1 
ATOM   313  C  C   . VAL   A 1 49  ? 30.965 -35.338 34.342  1.00 47.35  ? 742  VAL   A C   1 
ATOM   314  O  O   . VAL   A 1 49  ? 31.577 -35.835 35.284  1.00 47.56  ? 742  VAL   A O   1 
ATOM   315  C  CB  . VAL   A 1 49  ? 30.870 -35.881 31.826  1.00 49.39  ? 742  VAL   A CB  1 
ATOM   316  C  CG1 . VAL   A 1 49  ? 31.516 -35.646 30.469  1.00 49.59  ? 742  VAL   A CG1 1 
ATOM   317  C  CG2 . VAL   A 1 49  ? 30.720 -37.368 32.121  1.00 49.39  ? 742  VAL   A CG2 1 
ATOM   318  N  N   . ALA   A 1 50  ? 29.710 -34.856 34.466  1.00 45.27  ? 743  ALA   A N   1 
ATOM   319  C  CA  . ALA   A 1 50  ? 28.832 -35.015 35.620  1.00 43.49  ? 743  ALA   A CA  1 
ATOM   320  C  C   . ALA   A 1 50  ? 27.592 -35.687 35.051  1.00 42.20  ? 743  ALA   A C   1 
ATOM   321  O  O   . ALA   A 1 50  ? 27.059 -35.266 34.021  1.00 42.17  ? 743  ALA   A O   1 
ATOM   322  C  CB  . ALA   A 1 50  ? 28.473 -33.672 36.236  1.00 42.92  ? 743  ALA   A CB  1 
ATOM   323  N  N   . ILE   A 1 51  ? 27.184 -36.784 35.671  1.00 41.00  ? 744  ILE   A N   1 
ATOM   324  C  CA  . ILE   A 1 51  ? 26.048 -37.558 35.207  1.00 40.23  ? 744  ILE   A CA  1 
ATOM   325  C  C   . ILE   A 1 51  ? 24.917 -37.452 36.209  1.00 39.22  ? 744  ILE   A C   1 
ATOM   326  O  O   . ILE   A 1 51  ? 25.110 -37.777 37.370  1.00 38.77  ? 744  ILE   A O   1 
ATOM   327  C  CB  . ILE   A 1 51  ? 26.473 -39.029 35.009  1.00 40.18  ? 744  ILE   A CB  1 
ATOM   328  C  CG1 . ILE   A 1 51  ? 27.650 -39.131 34.033  1.00 40.95  ? 744  ILE   A CG1 1 
ATOM   329  C  CG2 . ILE   A 1 51  ? 25.302 -39.865 34.545  1.00 40.43  ? 744  ILE   A CG2 1 
ATOM   330  C  CD1 . ILE   A 1 51  ? 28.728 -39.998 34.512  1.00 42.12  ? 744  ILE   A CD1 1 
ATOM   331  N  N   . LYS   A 1 52  ? 23.748 -36.986 35.769  1.00 38.38  ? 745  LYS   A N   1 
ATOM   332  C  CA  . LYS   A 1 52  ? 22.592 -36.897 36.640  1.00 38.04  ? 745  LYS   A CA  1 
ATOM   333  C  C   . LYS   A 1 52  ? 21.675 -38.021 36.272  1.00 38.12  ? 745  LYS   A C   1 
ATOM   334  O  O   . LYS   A 1 52  ? 21.176 -38.075 35.156  1.00 38.11  ? 745  LYS   A O   1 
ATOM   335  C  CB  . LYS   A 1 52  ? 21.864 -35.551 36.503  1.00 39.18  ? 745  LYS   A CB  1 
ATOM   336  C  CG  . LYS   A 1 52  ? 20.586 -35.490 37.339  1.00 41.53  ? 745  LYS   A CG  1 
ATOM   337  C  CD  . LYS   A 1 52  ? 20.489 -34.257 38.173  1.00 44.51  ? 745  LYS   A CD  1 
ATOM   338  C  CE  . LYS   A 1 52  ? 19.962 -33.111 37.362  1.00 47.65  ? 745  LYS   A CE  1 
ATOM   339  N  NZ  . LYS   A 1 52  ? 19.978 -31.862 38.143  1.00 50.36  ? 745  LYS   A NZ  1 
ATOM   340  N  N   . GLU   A 1 53  ? 21.491 -38.943 37.194  1.00 38.58  ? 746  GLU   A N   1 
ATOM   341  C  CA  . GLU   A 1 53  ? 20.613 -40.068 36.980  1.00 39.62  ? 746  GLU   A CA  1 
ATOM   342  C  C   . GLU   A 1 53  ? 19.320 -39.758 37.703  1.00 40.70  ? 746  GLU   A C   1 
ATOM   343  O  O   . GLU   A 1 53  ? 19.275 -39.741 38.938  1.00 40.72  ? 746  GLU   A O   1 
ATOM   344  C  CB  . GLU   A 1 53  ? 21.247 -41.362 37.490  1.00 41.33  ? 746  GLU   A CB  1 
ATOM   345  C  CG  . GLU   A 1 53  ? 20.488 -42.574 37.021  1.00 45.29  ? 746  GLU   A CG  1 
ATOM   346  C  CD  . GLU   A 1 53  ? 21.166 -43.884 37.341  1.00 49.67  ? 746  GLU   A CD  1 
ATOM   347  O  OE1 . GLU   A 1 53  ? 21.794 -43.983 38.424  1.00 49.69  ? 746  GLU   A OE1 1 
ATOM   348  O  OE2 . GLU   A 1 53  ? 21.056 -44.818 36.510  1.00 51.25  ? 746  GLU   A OE2 1 
ATOM   349  N  N   . LEU   A 1 54  ? 18.284 -39.423 36.931  1.00 41.51  ? 747  LEU   A N   1 
ATOM   350  C  CA  . LEU   A 1 54  ? 17.002 -39.079 37.512  1.00 42.94  ? 747  LEU   A CA  1 
ATOM   351  C  C   . LEU   A 1 54  ? 16.384 -40.314 38.111  1.00 44.33  ? 747  LEU   A C   1 
ATOM   352  O  O   . LEU   A 1 54  ? 16.533 -41.426 37.564  1.00 45.11  ? 747  LEU   A O   1 
ATOM   353  C  CB  . LEU   A 1 54  ? 16.057 -38.514 36.446  1.00 43.35  ? 747  LEU   A CB  1 
ATOM   354  C  CG  . LEU   A 1 54  ? 16.526 -37.286 35.688  1.00 44.94  ? 747  LEU   A CG  1 
ATOM   355  C  CD1 . LEU   A 1 54  ? 15.507 -36.906 34.609  1.00 45.70  ? 747  LEU   A CD1 1 
ATOM   356  C  CD2 . LEU   A 1 54  ? 16.766 -36.118 36.637  1.00 45.18  ? 747  LEU   A CD2 1 
ATOM   357  N  N   . ARG   A 1 55  ? 15.605 -40.106 39.183  1.00 44.20  ? 748  ARG   A N   1 
ATOM   358  C  CA  . ARG   A 1 55  ? 14.867 -41.128 39.901  1.00 44.84  ? 748  ARG   A CA  1 
ATOM   359  C  C   . ARG   A 1 55  ? 14.000 -41.907 38.904  1.00 44.31  ? 748  ARG   A C   1 
ATOM   360  O  O   . ARG   A 1 55  ? 13.387 -41.282 38.045  1.00 44.30  ? 748  ARG   A O   1 
ATOM   361  C  CB  . ARG   A 1 55  ? 14.015 -40.460 41.007  1.00 47.31  ? 748  ARG   A CB  1 
ATOM   362  C  CG  . ARG   A 1 55  ? 13.318 -41.449 41.944  1.00 53.09  ? 748  ARG   A CG  1 
ATOM   363  C  CD  . ARG   A 1 55  ? 12.485 -40.760 43.013  1.00 58.08  ? 748  ARG   A CD  1 
ATOM   364  N  NE  . ARG   A 1 55  ? 11.294 -41.537 43.361  1.00 61.84  ? 748  ARG   A NE  1 
ATOM   365  C  CZ  . ARG   A 1 55  ? 11.236 -42.415 44.358  1.00 64.77  ? 748  ARG   A CZ  1 
ATOM   366  N  NH1 . ARG   A 1 55  ? 10.111 -43.072 44.608  1.00 64.83  ? 748  ARG   A NH1 1 
ATOM   367  N  NH2 . ARG   A 1 55  ? 12.301 -42.638 45.120  1.00 64.51  ? 748  ARG   A NH2 1 
ATOM   368  N  N   . GLU   A 1 56  ? 14.074 -43.247 38.923  1.00 43.68  ? 749  GLU   A N   1 
ATOM   369  C  CA  . GLU   A 1 56  ? 13.345 -44.107 37.996  1.00 43.47  ? 749  GLU   A CA  1 
ATOM   370  C  C   . GLU   A 1 56  ? 11.850 -43.891 38.066  1.00 43.97  ? 749  GLU   A C   1 
ATOM   371  O  O   . GLU   A 1 56  ? 11.337 -43.514 39.118  1.00 44.34  ? 749  GLU   A O   1 
ATOM   372  C  CB  . GLU   A 1 56  ? 13.696 -45.573 38.261  1.00 44.33  ? 749  GLU   A CB  1 
ATOM   373  C  CG  . GLU   A 1 56  ? 13.369 -46.492 37.112  1.00 47.69  ? 749  GLU   A CG  1 
ATOM   374  C  CD  . GLU   A 1 56  ? 13.761 -47.930 37.350  1.00 52.29  ? 749  GLU   A CD  1 
ATOM   375  O  OE1 . GLU   A 1 56  ? 14.654 -48.178 38.193  1.00 52.42  ? 749  GLU   A OE1 1 
ATOM   376  O  OE2 . GLU   A 1 56  ? 13.166 -48.822 36.705  1.00 54.25  ? 749  GLU   A OE2 1 
ATOM   377  N  N   . ALA   A 1 57  ? 11.161 -44.086 36.935  1.00 44.07  ? 750  ALA   A N   1 
ATOM   378  C  CA  . ALA   A 1 57  ? 9.718  -43.930 36.781  1.00 44.99  ? 750  ALA   A CA  1 
ATOM   379  C  C   . ALA   A 1 57  ? 9.190  -42.566 37.234  1.00 46.55  ? 750  ALA   A C   1 
ATOM   380  O  O   . ALA   A 1 57  ? 8.091  -42.476 37.785  1.00 46.67  ? 750  ALA   A O   1 
ATOM   381  C  CB  . ALA   A 1 57  ? 8.985  -45.066 37.480  1.00 44.85  ? 750  ALA   A CB  1 
ATOM   382  N  N   . THR   A 1 58  ? 9.982  -41.506 37.015  1.00 47.64  ? 751  THR   A N   1 
ATOM   383  C  CA  . THR   A 1 58  ? 9.614  -40.135 37.373  1.00 49.16  ? 751  THR   A CA  1 
ATOM   384  C  C   . THR   A 1 58  ? 8.889  -39.436 36.210  1.00 51.10  ? 751  THR   A C   1 
ATOM   385  O  O   . THR   A 1 58  ? 7.967  -38.645 36.442  1.00 51.22  ? 751  THR   A O   1 
ATOM   386  C  CB  . THR   A 1 58  ? 10.866 -39.370 37.810  1.00 50.09  ? 751  THR   A CB  1 
ATOM   387  O  OG1 . THR   A 1 58  ? 11.269 -39.875 39.070  1.00 51.61  ? 751  THR   A OG1 1 
ATOM   388  C  CG2 . THR   A 1 58  ? 10.633 -37.907 37.970  1.00 50.40  ? 751  THR   A CG2 1 
ATOM   389  N  N   . SER   A 1 59  ? 9.277  -39.754 34.956  1.00 52.22  ? 752  SER   A N   1 
ATOM   390  C  CA  . SER   A 1 59  ? 8.672  -39.089 33.809  1.00 53.68  ? 752  SER   A CA  1 
ATOM   391  C  C   . SER   A 1 59  ? 7.498  -39.813 33.162  1.00 54.29  ? 752  SER   A C   1 
ATOM   392  O  O   . SER   A 1 59  ? 7.623  -40.970 32.762  1.00 54.22  ? 752  SER   A O   1 
ATOM   393  C  CB  . SER   A 1 59  ? 9.718  -38.782 32.753  1.00 55.52  ? 752  SER   A CB  1 
ATOM   394  O  OG  . SER   A 1 59  ? 9.155  -37.937 31.763  1.00 57.96  ? 752  SER   A OG  1 
ATOM   395  N  N   . PRO   A 1 60  ? 6.391  -39.074 32.933  1.00 54.49  ? 753  PRO   A N   1 
ATOM   396  C  CA  . PRO   A 1 60  ? 5.214  -39.677 32.289  1.00 54.89  ? 753  PRO   A CA  1 
ATOM   397  C  C   . PRO   A 1 60  ? 5.271  -39.650 30.763  1.00 55.82  ? 753  PRO   A C   1 
ATOM   398  O  O   . PRO   A 1 60  ? 4.236  -39.495 30.115  1.00 56.15  ? 753  PRO   A O   1 
ATOM   399  C  CB  . PRO   A 1 60  ? 4.089  -38.768 32.760  1.00 55.40  ? 753  PRO   A CB  1 
ATOM   400  C  CG  . PRO   A 1 60  ? 4.726  -37.443 32.833  1.00 55.52  ? 753  PRO   A CG  1 
ATOM   401  C  CD  . PRO   A 1 60  ? 6.119  -37.682 33.341  1.00 53.82  ? 753  PRO   A CD  1 
ATOM   402  N  N   . LYS   A 1 61  ? 6.470  -39.742 30.189  1.00 55.97  ? 754  LYS   A N   1 
ATOM   403  C  CA  . LYS   A 1 61  ? 6.643  -39.684 28.743  1.00 56.30  ? 754  LYS   A CA  1 
ATOM   404  C  C   . LYS   A 1 61  ? 7.377  -40.899 28.230  1.00 56.62  ? 754  LYS   A C   1 
ATOM   405  O  O   . LYS   A 1 61  ? 8.276  -41.404 28.898  1.00 56.84  ? 754  LYS   A O   1 
ATOM   406  C  CB  . LYS   A 1 61  ? 7.435  -38.425 28.360  1.00 57.99  ? 754  LYS   A CB  1 
ATOM   407  C  CG  . LYS   A 1 61  ? 6.696  -37.140 28.669  1.00 61.74  ? 754  LYS   A CG  1 
ATOM   408  C  CD  . LYS   A 1 61  ? 7.628  -35.994 28.952  1.00 65.50  ? 754  LYS   A CD  1 
ATOM   409  C  CE  . LYS   A 1 61  ? 6.853  -34.712 28.967  1.00 69.43  ? 754  LYS   A CE  1 
ATOM   410  N  NZ  . LYS   A 1 61  ? 6.395  -34.345 27.601  1.00 72.01  ? 754  LYS   A NZ  1 
ATOM   411  N  N   . ALA   A 1 62  ? 7.027  -41.353 27.023  1.00 56.55  ? 755  ALA   A N   1 
ATOM   412  C  CA  . ALA   A 1 62  ? 7.715  -42.486 26.397  1.00 56.75  ? 755  ALA   A CA  1 
ATOM   413  C  C   . ALA   A 1 62  ? 9.127  -42.050 25.953  1.00 56.76  ? 755  ALA   A C   1 
ATOM   414  O  O   . ALA   A 1 62  ? 9.386  -40.849 25.806  1.00 56.79  ? 755  ALA   A O   1 
ATOM   415  C  CB  . ALA   A 1 62  ? 6.916  -42.989 25.205  1.00 56.83  ? 755  ALA   A CB  1 
ATOM   416  N  N   . ASN   A 1 63  ? 10.038 -43.012 25.733  1.00 56.43  ? 756  ASN   A N   1 
ATOM   417  C  CA  . ASN   A 1 63  ? 11.419 -42.700 25.360  1.00 56.41  ? 756  ASN   A CA  1 
ATOM   418  C  C   . ASN   A 1 63  ? 11.556 -41.778 24.139  1.00 56.22  ? 756  ASN   A C   1 
ATOM   419  O  O   . ASN   A 1 63  ? 12.544 -41.052 24.061  1.00 56.45  ? 756  ASN   A O   1 
ATOM   420  C  CB  . ASN   A 1 63  ? 12.255 -43.970 25.193  1.00 57.37  ? 756  ASN   A CB  1 
ATOM   421  C  CG  . ASN   A 1 63  ? 12.826 -44.528 26.483  1.00 60.32  ? 756  ASN   A CG  1 
ATOM   422  O  OD1 . ASN   A 1 63  ? 13.729 -45.381 26.463  1.00 61.88  ? 756  ASN   A OD1 1 
ATOM   423  N  ND2 . ASN   A 1 63  ? 12.329 -44.072 27.638  1.00 60.40  ? 756  ASN   A ND2 1 
ATOM   424  N  N   . LYS   A 1 64  ? 10.564 -41.748 23.232  1.00 55.68  ? 757  LYS   A N   1 
ATOM   425  C  CA  . LYS   A 1 64  ? 10.636 -40.850 22.083  1.00 55.57  ? 757  LYS   A CA  1 
ATOM   426  C  C   . LYS   A 1 64  ? 10.337 -39.429 22.502  1.00 54.59  ? 757  LYS   A C   1 
ATOM   427  O  O   . LYS   A 1 64  ? 11.024 -38.518 22.054  1.00 54.72  ? 757  LYS   A O   1 
ATOM   428  C  CB  . LYS   A 1 64  ? 9.731  -41.304 20.934  1.00 58.48  ? 757  LYS   A CB  1 
ATOM   429  C  CG  . LYS   A 1 64  ? 10.097 -42.684 20.374  1.00 64.57  ? 757  LYS   A CG  1 
ATOM   430  C  CD  . LYS   A 1 64  ? 11.364 -42.712 19.496  1.00 69.74  ? 757  LYS   A CD  1 
ATOM   431  C  CE  . LYS   A 1 64  ? 12.562 -43.335 20.183  1.00 73.54  ? 757  LYS   A CE  1 
ATOM   432  N  NZ  . LYS   A 1 64  ? 12.197 -44.555 20.957  1.00 75.79  ? 757  LYS   A NZ  1 
ATOM   433  N  N   . GLU   A 1 65  ? 9.356  -39.226 23.387  1.00 53.62  ? 758  GLU   A N   1 
ATOM   434  C  CA  . GLU   A 1 65  ? 9.028  -37.880 23.861  1.00 53.28  ? 758  GLU   A CA  1 
ATOM   435  C  C   . GLU   A 1 65  ? 10.077 -37.318 24.800  1.00 52.58  ? 758  GLU   A C   1 
ATOM   436  O  O   . GLU   A 1 65  ? 10.241 -36.101 24.851  1.00 52.88  ? 758  GLU   A O   1 
ATOM   437  C  CB  . GLU   A 1 65  ? 7.644  -37.812 24.501  1.00 55.77  ? 758  GLU   A CB  1 
ATOM   438  C  CG  . GLU   A 1 65  ? 6.527  -37.904 23.484  1.00 61.49  ? 758  GLU   A CG  1 
ATOM   439  C  CD  . GLU   A 1 65  ? 6.092  -39.324 23.195  1.00 69.45  ? 758  GLU   A CD  1 
ATOM   440  O  OE1 . GLU   A 1 65  ? 6.334  -39.805 22.063  1.00 69.77  ? 758  GLU   A OE1 1 
ATOM   441  O  OE2 . GLU   A 1 65  ? 5.520  -39.960 24.111  1.00 73.67  ? 758  GLU   A OE2 1 
ATOM   442  N  N   . ILE   A 1 66  ? 10.809 -38.189 25.525  1.00 51.72  ? 759  ILE   A N   1 
ATOM   443  C  CA  . ILE   A 1 66  ? 11.906 -37.769 26.400  1.00 51.39  ? 759  ILE   A CA  1 
ATOM   444  C  C   . ILE   A 1 66  ? 13.011 -37.197 25.506  1.00 51.12  ? 759  ILE   A C   1 
ATOM   445  O  O   . ILE   A 1 66  ? 13.456 -36.080 25.722  1.00 51.54  ? 759  ILE   A O   1 
ATOM   446  C  CB  . ILE   A 1 66  ? 12.411 -38.946 27.282  1.00 51.55  ? 759  ILE   A CB  1 
ATOM   447  C  CG1 . ILE   A 1 66  ? 11.402 -39.277 28.372  1.00 52.50  ? 759  ILE   A CG1 1 
ATOM   448  C  CG2 . ILE   A 1 66  ? 13.777 -38.652 27.897  1.00 51.75  ? 759  ILE   A CG2 1 
ATOM   449  C  CD1 . ILE   A 1 66  ? 11.673 -40.558 29.073  1.00 53.75  ? 759  ILE   A CD1 1 
ATOM   450  N  N   . LEU   A 1 67  ? 13.370 -37.929 24.451  1.00 50.19  ? 760  LEU   A N   1 
ATOM   451  C  CA  . LEU   A 1 67  ? 14.368 -37.531 23.473  1.00 50.08  ? 760  LEU   A CA  1 
ATOM   452  C  C   . LEU   A 1 67  ? 14.007 -36.218 22.754  1.00 50.46  ? 760  LEU   A C   1 
ATOM   453  O  O   . LEU   A 1 67  ? 14.897 -35.435 22.440  1.00 50.73  ? 760  LEU   A O   1 
ATOM   454  C  CB  . LEU   A 1 67  ? 14.551 -38.679 22.457  1.00 49.88  ? 760  LEU   A CB  1 
ATOM   455  C  CG  . LEU   A 1 67  ? 15.794 -39.606 22.542  1.00 50.58  ? 760  LEU   A CG  1 
ATOM   456  C  CD1 . LEU   A 1 67  ? 16.637 -39.416 23.820  1.00 50.87  ? 760  LEU   A CD1 1 
ATOM   457  C  CD2 . LEU   A 1 67  ? 15.416 -41.051 22.330  1.00 50.96  ? 760  LEU   A CD2 1 
ATOM   458  N  N   . ASP   A 1 68  ? 12.712 -35.966 22.521  1.00 50.26  ? 761  ASP   A N   1 
ATOM   459  C  CA  . ASP   A 1 68  ? 12.242 -34.735 21.893  1.00 50.49  ? 761  ASP   A CA  1 
ATOM   460  C  C   . ASP   A 1 68  ? 12.540 -33.545 22.814  1.00 50.40  ? 761  ASP   A C   1 
ATOM   461  O  O   . ASP   A 1 68  ? 12.998 -32.506 22.345  1.00 50.29  ? 761  ASP   A O   1 
ATOM   462  C  CB  . ASP   A 1 68  ? 10.727 -34.810 21.602  1.00 52.53  ? 761  ASP   A CB  1 
ATOM   463  C  CG  . ASP   A 1 68  ? 10.342 -35.733 20.462  1.00 57.99  ? 761  ASP   A CG  1 
ATOM   464  O  OD1 . ASP   A 1 68  ? 11.250 -36.166 19.713  1.00 58.82  ? 761  ASP   A OD1 1 
ATOM   465  O  OD2 . ASP   A 1 68  ? 9.131  -36.036 20.324  1.00 60.45  ? 761  ASP   A OD2 1 
ATOM   466  N  N   . GLU   A 1 69  ? 12.278 -33.716 24.126  1.00 50.18  ? 762  GLU   A N   1 
ATOM   467  C  CA  . GLU   A 1 69  ? 12.533 -32.719 25.174  1.00 50.43  ? 762  GLU   A CA  1 
ATOM   468  C  C   . GLU   A 1 69  ? 14.039 -32.498 25.319  1.00 49.05  ? 762  GLU   A C   1 
ATOM   469  O  O   . GLU   A 1 69  ? 14.476 -31.363 25.478  1.00 48.96  ? 762  GLU   A O   1 
ATOM   470  C  CB  . GLU   A 1 69  ? 11.974 -33.218 26.530  1.00 54.44  ? 762  GLU   A CB  1 
ATOM   471  C  CG  . GLU   A 1 69  ? 10.767 -32.466 27.052  1.00 62.37  ? 762  GLU   A CG  1 
ATOM   472  C  CD  . GLU   A 1 69  ? 9.579  -32.533 26.114  1.00 72.35  ? 762  GLU   A CD  1 
ATOM   473  O  OE1 . GLU   A 1 69  ? 9.329  -31.525 25.413  1.00 75.03  ? 762  GLU   A OE1 1 
ATOM   474  O  OE2 . GLU   A 1 69  ? 8.910  -33.593 26.065  1.00 74.49  ? 762  GLU   A OE2 1 
ATOM   475  N  N   . ALA   A 1 70  ? 14.817 -33.597 25.278  1.00 47.89  ? 763  ALA   A N   1 
ATOM   476  C  CA  . ALA   A 1 70  ? 16.262 -33.619 25.399  1.00 47.73  ? 763  ALA   A CA  1 
ATOM   477  C  C   . ALA   A 1 70  ? 16.902 -32.867 24.253  1.00 48.30  ? 763  ALA   A C   1 
ATOM   478  O  O   . ALA   A 1 70  ? 17.881 -32.160 24.486  1.00 48.44  ? 763  ALA   A O   1 
ATOM   479  C  CB  . ALA   A 1 70  ? 16.759 -35.051 25.435  1.00 47.70  ? 763  ALA   A CB  1 
ATOM   480  N  N   . TYR   A 1 71  ? 16.333 -32.975 23.021  1.00 48.45  ? 764  TYR   A N   1 
ATOM   481  C  CA  . TYR   A 1 71  ? 16.800 -32.250 21.834  1.00 48.77  ? 764  TYR   A CA  1 
ATOM   482  C  C   . TYR   A 1 71  ? 16.565 -30.749 22.037  1.00 47.05  ? 764  TYR   A C   1 
ATOM   483  O  O   . TYR   A 1 71  ? 17.435 -29.948 21.734  1.00 47.19  ? 764  TYR   A O   1 
ATOM   484  C  CB  . TYR   A 1 71  ? 16.076 -32.744 20.566  1.00 50.29  ? 764  TYR   A CB  1 
ATOM   485  C  CG  . TYR   A 1 71  ? 16.495 -32.031 19.292  1.00 52.93  ? 764  TYR   A CG  1 
ATOM   486  C  CD1 . TYR   A 1 71  ? 15.928 -30.811 18.931  1.00 54.40  ? 764  TYR   A CD1 1 
ATOM   487  C  CD2 . TYR   A 1 71  ? 17.428 -32.594 18.429  1.00 54.61  ? 764  TYR   A CD2 1 
ATOM   488  C  CE1 . TYR   A 1 71  ? 16.326 -30.142 17.780  1.00 55.76  ? 764  TYR   A CE1 1 
ATOM   489  C  CE2 . TYR   A 1 71  ? 17.811 -31.947 17.257  1.00 55.89  ? 764  TYR   A CE2 1 
ATOM   490  C  CZ  . TYR   A 1 71  ? 17.252 -30.724 16.932  1.00 56.99  ? 764  TYR   A CZ  1 
ATOM   491  O  OH  . TYR   A 1 71  ? 17.634 -30.077 15.778  1.00 58.74  ? 764  TYR   A OH  1 
ATOM   492  N  N   . VAL   A 1 72  ? 15.406 -30.374 22.567  1.00 45.63  ? 765  VAL   A N   1 
ATOM   493  C  CA  . VAL   A 1 72  ? 15.090 -28.982 22.863  1.00 45.04  ? 765  VAL   A CA  1 
ATOM   494  C  C   . VAL   A 1 72  ? 15.992 -28.428 23.999  1.00 44.39  ? 765  VAL   A C   1 
ATOM   495  O  O   . VAL   A 1 72  ? 16.289 -27.247 24.023  1.00 44.44  ? 765  VAL   A O   1 
ATOM   496  C  CB  . VAL   A 1 72  ? 13.581 -28.824 23.152  1.00 45.69  ? 765  VAL   A CB  1 
ATOM   497  C  CG1 . VAL   A 1 72  ? 13.236 -27.390 23.521  1.00 46.49  ? 765  VAL   A CG1 1 
ATOM   498  C  CG2 . VAL   A 1 72  ? 12.764 -29.262 21.950  1.00 46.13  ? 765  VAL   A CG2 1 
ATOM   499  N  N   . MET   A 1 73  ? 16.471 -29.288 24.902  1.00 43.62  ? 766  MET   A N   1 
ATOM   500  C  CA  . MET   A 1 73  ? 17.405 -28.900 25.957  1.00 42.95  ? 766  MET   A CA  1 
ATOM   501  C  C   . MET   A 1 73  ? 18.800 -28.718 25.361  1.00 42.44  ? 766  MET   A C   1 
ATOM   502  O  O   . MET   A 1 73  ? 19.534 -27.826 25.777  1.00 42.71  ? 766  MET   A O   1 
ATOM   503  C  CB  . MET   A 1 73  ? 17.472 -29.984 27.031  1.00 43.32  ? 766  MET   A CB  1 
ATOM   504  C  CG  . MET   A 1 73  ? 16.333 -29.974 27.976  1.00 44.75  ? 766  MET   A CG  1 
ATOM   505  S  SD  . MET   A 1 73  ? 16.581 -31.275 29.195  1.00 48.00  ? 766  MET   A SD  1 
ATOM   506  C  CE  . MET   A 1 73  ? 15.191 -32.257 28.825  1.00 49.41  ? 766  MET   A CE  1 
ATOM   507  N  N   . ALA   A 1 74  ? 19.190 -29.585 24.419  1.00 41.72  ? 767  ALA   A N   1 
ATOM   508  C  CA  . ALA   A 1 74  ? 20.487 -29.457 23.764  1.00 41.66  ? 767  ALA   A CA  1 
ATOM   509  C  C   . ALA   A 1 74  ? 20.498 -28.245 22.801  1.00 41.92  ? 767  ALA   A C   1 
ATOM   510  O  O   . ALA   A 1 74  ? 21.546 -27.638 22.586  1.00 42.05  ? 767  ALA   A O   1 
ATOM   511  C  CB  . ALA   A 1 74  ? 20.820 -30.735 23.022  1.00 41.30  ? 767  ALA   A CB  1 
ATOM   512  N  N   . SER   A 1 75  ? 19.328 -27.885 22.239  1.00 41.72  ? 768  SER   A N   1 
ATOM   513  C  CA  . SER   A 1 75  ? 19.194 -26.781 21.300  1.00 41.96  ? 768  SER   A CA  1 
ATOM   514  C  C   . SER   A 1 75  ? 19.422 -25.407 21.937  1.00 42.02  ? 768  SER   A C   1 
ATOM   515  O  O   . SER   A 1 75  ? 19.713 -24.448 21.215  1.00 42.60  ? 768  SER   A O   1 
ATOM   516  C  CB  . SER   A 1 75  ? 17.857 -26.846 20.570  1.00 43.35  ? 768  SER   A CB  1 
ATOM   517  O  OG  . SER   A 1 75  ? 16.810 -26.236 21.306  1.00 45.82  ? 768  SER   A OG  1 
ATOM   518  N  N   . VAL   A 1 76  ? 19.316 -25.304 23.277  1.00 41.35  ? 769  VAL   A N   1 
ATOM   519  C  CA  . VAL   A 1 76  ? 19.596 -24.037 23.955  1.00 41.22  ? 769  VAL   A CA  1 
ATOM   520  C  C   . VAL   A 1 76  ? 21.082 -23.640 23.797  1.00 40.94  ? 769  VAL   A C   1 
ATOM   521  O  O   . VAL   A 1 76  ? 21.411 -22.465 23.922  1.00 40.41  ? 769  VAL   A O   1 
ATOM   522  C  CB  . VAL   A 1 76  ? 19.137 -23.976 25.440  1.00 41.64  ? 769  VAL   A CB  1 
ATOM   523  C  CG1 . VAL   A 1 76  ? 17.808 -24.687 25.655  1.00 41.42  ? 769  VAL   A CG1 1 
ATOM   524  C  CG2 . VAL   A 1 76  ? 20.217 -24.504 26.379  1.00 42.36  ? 769  VAL   A CG2 1 
ATOM   525  N  N   . ASP   A 1 77  ? 21.978 -24.619 23.540  1.00 41.11  ? 770  ASP   A N   1 
ATOM   526  C  CA  . ASP   A 1 77  ? 23.382 -24.306 23.302  1.00 41.74  ? 770  ASP   A CA  1 
ATOM   527  C  C   . ASP   A 1 77  ? 23.622 -23.650 21.913  1.00 41.54  ? 770  ASP   A C   1 
ATOM   528  O  O   . ASP   A 1 77  ? 24.757 -23.308 21.578  1.00 41.90  ? 770  ASP   A O   1 
ATOM   529  C  CB  . ASP   A 1 77  ? 24.292 -25.516 23.532  1.00 43.93  ? 770  ASP   A CB  1 
ATOM   530  C  CG  . ASP   A 1 77  ? 25.723 -25.080 23.740  1.00 50.32  ? 770  ASP   A CG  1 
ATOM   531  O  OD1 . ASP   A 1 77  ? 25.937 -24.078 24.461  1.00 51.71  ? 770  ASP   A OD1 1 
ATOM   532  O  OD2 . ASP   A 1 77  ? 26.629 -25.706 23.146  1.00 53.45  ? 770  ASP   A OD2 1 
ATOM   533  N  N   . ASN   A 1 78  ? 22.552 -23.388 21.151  1.00 40.67  ? 771  ASN   A N   1 
ATOM   534  C  CA  . ASN   A 1 78  ? 22.661 -22.701 19.883  1.00 40.48  ? 771  ASN   A CA  1 
ATOM   535  C  C   . ASN   A 1 78  ? 21.801 -21.409 19.890  1.00 40.13  ? 771  ASN   A C   1 
ATOM   536  O  O   . ASN   A 1 78  ? 20.565 -21.479 19.907  1.00 40.48  ? 771  ASN   A O   1 
ATOM   537  C  CB  . ASN   A 1 78  ? 22.258 -23.628 18.759  1.00 41.28  ? 771  ASN   A CB  1 
ATOM   538  C  CG  . ASN   A 1 78  ? 22.561 -23.077 17.408  1.00 44.10  ? 771  ASN   A CG  1 
ATOM   539  O  OD1 . ASN   A 1 78  ? 23.437 -22.246 17.241  1.00 45.88  ? 771  ASN   A OD1 1 
ATOM   540  N  ND2 . ASN   A 1 78  ? 21.842 -23.532 16.410  1.00 44.56  ? 771  ASN   A ND2 1 
ATOM   541  N  N   . PRO   A 1 79  ? 22.432 -20.219 19.923  1.00 38.97  ? 772  PRO   A N   1 
ATOM   542  C  CA  . PRO   A 1 79  ? 23.885 -19.960 19.858  1.00 38.59  ? 772  PRO   A CA  1 
ATOM   543  C  C   . PRO   A 1 79  ? 24.656 -20.077 21.190  1.00 38.18  ? 772  PRO   A C   1 
ATOM   544  O  O   . PRO   A 1 79  ? 25.888 -20.006 21.203  1.00 38.20  ? 772  PRO   A O   1 
ATOM   545  C  CB  . PRO   A 1 79  ? 23.939 -18.553 19.264  1.00 39.24  ? 772  PRO   A CB  1 
ATOM   546  C  CG  . PRO   A 1 79  ? 22.714 -17.889 19.833  1.00 39.82  ? 772  PRO   A CG  1 
ATOM   547  C  CD  . PRO   A 1 79  ? 21.660 -18.964 19.907  1.00 38.21  ? 772  PRO   A CD  1 
ATOM   548  N  N   . GLY   A 1 80  ? 23.925 -20.279 22.288  1.00 37.48  ? 773  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 80  ? 24.489 -20.470 23.617  1.00 37.29  ? 773  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 80  ? 24.641 -19.200 24.423  1.00 36.82  ? 773  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 80  ? 24.416 -18.114 23.910  1.00 37.36  ? 773  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 81  ? 25.034 -19.333 25.688  1.00 36.07  ? 774  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 81  ? 25.300 -18.253 26.638  1.00 35.93  ? 774  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 81  ? 26.266 -18.796 27.687  1.00 35.62  ? 774  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 81  ? 26.004 -19.869 28.219  1.00 36.04  ? 774  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 81  ? 24.015 -17.823 27.313  1.00 37.15  ? 774  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 81  ? 24.169 -16.577 28.128  1.00 40.20  ? 774  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 81  ? 24.121 -15.473 27.616  1.00 41.56  ? 774  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 81  ? 24.365 -16.727 29.415  1.00 41.56  ? 774  ASN   A ND2 1 
ATOM   560  N  N   . PRO   A 1 82  ? 27.366 -18.100 28.033  1.00 35.05  ? 775  PRO   A N   1 
ATOM   561  C  CA  . PRO   A 1 82  ? 28.308 -18.671 29.015  1.00 34.80  ? 775  PRO   A CA  1 
ATOM   562  C  C   . PRO   A 1 82  ? 27.731 -18.934 30.393  1.00 34.94  ? 775  PRO   A C   1 
ATOM   563  O  O   . PRO   A 1 82  ? 28.361 -19.629 31.171  1.00 34.73  ? 775  PRO   A O   1 
ATOM   564  C  CB  . PRO   A 1 82  ? 29.459 -17.661 29.067  1.00 35.32  ? 775  PRO   A CB  1 
ATOM   565  C  CG  . PRO   A 1 82  ? 28.965 -16.455 28.424  1.00 35.70  ? 775  PRO   A CG  1 
ATOM   566  C  CD  . PRO   A 1 82  ? 27.848 -16.816 27.499  1.00 34.49  ? 775  PRO   A CD  1 
ATOM   567  N  N   . HIS   A 1 83  ? 26.542 -18.402 30.696  1.00 35.27  ? 776  HIS   A N   1 
ATOM   568  C  CA  . HIS   A 1 83  ? 25.943 -18.581 32.013  1.00 35.65  ? 776  HIS   A CA  1 
ATOM   569  C  C   . HIS   A 1 83  ? 24.747 -19.531 32.022  1.00 35.93  ? 776  HIS   A C   1 
ATOM   570  O  O   . HIS   A 1 83  ? 23.932 -19.496 32.936  1.00 36.14  ? 776  HIS   A O   1 
ATOM   571  C  CB  . HIS   A 1 83  ? 25.604 -17.225 32.634  1.00 36.19  ? 776  HIS   A CB  1 
ATOM   572  C  CG  . HIS   A 1 83  ? 26.792 -16.321 32.662  1.00 38.07  ? 776  HIS   A CG  1 
ATOM   573  N  ND1 . HIS   A 1 83  ? 26.843 -15.176 31.895  1.00 39.80  ? 776  HIS   A ND1 1 
ATOM   574  C  CD2 . HIS   A 1 83  ? 27.983 -16.484 33.282  1.00 39.37  ? 776  HIS   A CD2 1 
ATOM   575  C  CE1 . HIS   A 1 83  ? 28.040 -14.648 32.109  1.00 40.37  ? 776  HIS   A CE1 1 
ATOM   576  N  NE2 . HIS   A 1 83  ? 28.761 -15.399 32.937  1.00 40.53  ? 776  HIS   A NE2 1 
ATOM   577  N  N   . VAL   A 1 84  ? 24.677 -20.422 31.049  1.00 36.06  ? 777  VAL   A N   1 
ATOM   578  C  CA  . VAL   A 1 84  ? 23.651 -21.459 30.967  1.00 36.78  ? 777  VAL   A CA  1 
ATOM   579  C  C   . VAL   A 1 84  ? 24.402 -22.777 30.678  1.00 38.24  ? 777  VAL   A C   1 
ATOM   580  O  O   . VAL   A 1 84  ? 25.250 -22.821 29.786  1.00 38.87  ? 777  VAL   A O   1 
ATOM   581  C  CB  . VAL   A 1 84  ? 22.573 -21.145 29.887  1.00 36.74  ? 777  VAL   A CB  1 
ATOM   582  C  CG1 . VAL   A 1 84  ? 21.556 -22.258 29.783  1.00 36.97  ? 777  VAL   A CG1 1 
ATOM   583  C  CG2 . VAL   A 1 84  ? 21.871 -19.829 30.162  1.00 36.87  ? 777  VAL   A CG2 1 
ATOM   584  N  N   . CYS   A 1 85  ? 24.129 -23.829 31.448  1.00 39.03  ? 778  CYS   A N   1 
ATOM   585  C  CA  . CYS   A 1 85  ? 24.783 -25.131 31.266  1.00 40.19  ? 778  CYS   A CA  1 
ATOM   586  C  C   . CYS   A 1 85  ? 24.510 -25.758 29.908  1.00 40.87  ? 778  CYS   A C   1 
ATOM   587  O  O   . CYS   A 1 85  ? 23.502 -25.440 29.269  1.00 41.40  ? 778  CYS   A O   1 
ATOM   588  C  CB  . CYS   A 1 85  ? 24.406 -26.085 32.394  1.00 41.12  ? 778  CYS   A CB  1 
ATOM   589  S  SG  . CYS   A 1 85  ? 25.119 -25.660 34.000  1.00 44.45  ? 778  CYS   A SG  1 
ATOM   590  N  N   . ARG   A 1 86  ? 25.404 -26.666 29.470  1.00 40.82  ? 779  ARG   A N   1 
ATOM   591  C  CA  . ARG   A 1 86  ? 25.256 -27.343 28.178  1.00 41.42  ? 779  ARG   A CA  1 
ATOM   592  C  C   . ARG   A 1 86  ? 24.886 -28.805 28.372  1.00 41.19  ? 779  ARG   A C   1 
ATOM   593  O  O   . ARG   A 1 86  ? 25.631 -29.523 29.050  1.00 41.21  ? 779  ARG   A O   1 
ATOM   594  C  CB  . ARG   A 1 86  ? 26.573 -27.299 27.390  1.00 43.80  ? 779  ARG   A CB  1 
ATOM   595  C  CG  . ARG   A 1 86  ? 27.104 -25.903 27.132  1.00 49.77  ? 779  ARG   A CG  1 
ATOM   596  C  CD  . ARG   A 1 86  ? 28.176 -25.931 26.060  1.00 55.37  ? 779  ARG   A CD  1 
ATOM   597  N  NE  . ARG   A 1 86  ? 29.524 -25.990 26.617  1.00 60.81  ? 779  ARG   A NE  1 
ATOM   598  C  CZ  . ARG   A 1 86  ? 30.474 -25.091 26.381  1.00 64.42  ? 779  ARG   A CZ  1 
ATOM   599  N  NH1 . ARG   A 1 86  ? 30.231 -24.046 25.592  1.00 64.10  ? 779  ARG   A NH1 1 
ATOM   600  N  NH2 . ARG   A 1 86  ? 31.673 -25.226 26.932  1.00 65.15  ? 779  ARG   A NH2 1 
ATOM   601  N  N   . LEU   A 1 87  ? 23.778 -29.270 27.753  1.00 40.71  ? 780  LEU   A N   1 
ATOM   602  C  CA  . LEU   A 1 87  ? 23.452 -30.693 27.860  1.00 40.58  ? 780  LEU   A CA  1 
ATOM   603  C  C   . LEU   A 1 87  ? 24.275 -31.430 26.801  1.00 41.62  ? 780  LEU   A C   1 
ATOM   604  O  O   . LEU   A 1 87  ? 23.955 -31.341 25.615  1.00 41.66  ? 780  LEU   A O   1 
ATOM   605  C  CB  . LEU   A 1 87  ? 21.957 -30.979 27.668  1.00 39.75  ? 780  LEU   A CB  1 
ATOM   606  C  CG  . LEU   A 1 87  ? 21.568 -32.460 27.788  1.00 39.64  ? 780  LEU   A CG  1 
ATOM   607  C  CD1 . LEU   A 1 87  ? 21.912 -33.018 29.168  1.00 39.57  ? 780  LEU   A CD1 1 
ATOM   608  C  CD2 . LEU   A 1 87  ? 20.105 -32.654 27.502  1.00 39.80  ? 780  LEU   A CD2 1 
ATOM   609  N  N   . LEU   A 1 88  ? 25.364 -32.099 27.212  1.00 42.26  ? 781  LEU   A N   1 
ATOM   610  C  CA  . LEU   A 1 88  ? 26.239 -32.824 26.285  1.00 43.23  ? 781  LEU   A CA  1 
ATOM   611  C  C   . LEU   A 1 88  ? 25.573 -34.047 25.648  1.00 43.70  ? 781  LEU   A C   1 
ATOM   612  O  O   . LEU   A 1 88  ? 25.777 -34.314 24.468  1.00 44.22  ? 781  LEU   A O   1 
ATOM   613  C  CB  . LEU   A 1 88  ? 27.523 -33.271 26.999  1.00 43.63  ? 781  LEU   A CB  1 
ATOM   614  C  CG  . LEU   A 1 88  ? 28.456 -32.165 27.456  1.00 45.22  ? 781  LEU   A CG  1 
ATOM   615  C  CD1 . LEU   A 1 88  ? 29.624 -32.750 28.221  1.00 46.01  ? 781  LEU   A CD1 1 
ATOM   616  C  CD2 . LEU   A 1 88  ? 28.956 -31.361 26.281  1.00 45.38  ? 781  LEU   A CD2 1 
ATOM   617  N  N   . GLY   A 1 89  ? 24.817 -34.792 26.434  1.00 43.42  ? 782  GLY   A N   1 
ATOM   618  C  CA  . GLY   A 1 89  ? 24.156 -35.990 25.946  1.00 43.73  ? 782  GLY   A CA  1 
ATOM   619  C  C   . GLY   A 1 89  ? 23.214 -36.631 26.941  1.00 43.88  ? 782  GLY   A C   1 
ATOM   620  O  O   . GLY   A 1 89  ? 23.192 -36.260 28.113  1.00 43.45  ? 782  GLY   A O   1 
ATOM   621  N  N   . ILE   A 1 90  ? 22.426 -37.598 26.465  1.00 44.04  ? 783  ILE   A N   1 
ATOM   622  C  CA  . ILE   A 1 90  ? 21.468 -38.323 27.285  1.00 44.76  ? 783  ILE   A CA  1 
ATOM   623  C  C   . ILE   A 1 90  ? 21.623 -39.823 27.088  1.00 45.12  ? 783  ILE   A C   1 
ATOM   624  O  O   . ILE   A 1 90  ? 21.920 -40.283 25.982  1.00 45.31  ? 783  ILE   A O   1 
ATOM   625  C  CB  . ILE   A 1 90  ? 20.034 -37.866 26.923  1.00 45.61  ? 783  ILE   A CB  1 
ATOM   626  C  CG1 . ILE   A 1 90  ? 18.968 -38.523 27.838  1.00 46.36  ? 783  ILE   A CG1 1 
ATOM   627  C  CG2 . ILE   A 1 90  ? 19.740 -38.078 25.424  1.00 46.13  ? 783  ILE   A CG2 1 
ATOM   628  C  CD1 . ILE   A 1 90  ? 17.541 -38.045 27.580  1.00 47.67  ? 783  ILE   A CD1 1 
ATOM   629  N  N   . CYS   A 1 91  ? 21.426 -40.592 28.155  1.00 44.97  ? 784  CYS   A N   1 
ATOM   630  C  CA  . CYS   A 1 91  ? 21.480 -42.047 28.086  1.00 45.17  ? 784  CYS   A CA  1 
ATOM   631  C  C   . CYS   A 1 91  ? 20.202 -42.626 28.683  1.00 45.42  ? 784  CYS   A C   1 
ATOM   632  O  O   . CYS   A 1 91  ? 19.958 -42.488 29.882  1.00 45.81  ? 784  CYS   A O   1 
ATOM   633  C  CB  . CYS   A 1 91  ? 22.719 -42.594 28.783  1.00 45.56  ? 784  CYS   A CB  1 
ATOM   634  S  SG  . CYS   A 1 91  ? 22.857 -44.399 28.730  1.00 48.75  ? 784  CYS   A SG  1 
ATOM   635  N  N   . LEU   A 1 92  ? 19.377 -43.260 27.841  1.00 45.17  ? 785  LEU   A N   1 
ATOM   636  C  CA  . LEU   A 1 92  ? 18.118 -43.867 28.276  1.00 45.13  ? 785  LEU   A CA  1 
ATOM   637  C  C   . LEU   A 1 92  ? 18.242 -45.373 28.543  1.00 45.80  ? 785  LEU   A C   1 
ATOM   638  O  O   . LEU   A 1 92  ? 18.475 -46.162 27.638  1.00 45.39  ? 785  LEU   A O   1 
ATOM   639  C  CB  . LEU   A 1 92  ? 16.990 -43.587 27.273  1.00 44.62  ? 785  LEU   A CB  1 
ATOM   640  C  CG  . LEU   A 1 92  ? 16.630 -42.124 27.026  1.00 44.96  ? 785  LEU   A CG  1 
ATOM   641  C  CD1 . LEU   A 1 92  ? 15.500 -42.024 26.012  1.00 44.58  ? 785  LEU   A CD1 1 
ATOM   642  C  CD2 . LEU   A 1 92  ? 16.257 -41.428 28.346  1.00 45.89  ? 785  LEU   A CD2 1 
ATOM   643  N  N   . THR   A 1 93  ? 18.143 -45.741 29.827  1.00 46.69  ? 786  THR   A N   1 
ATOM   644  C  CA  . THR   A 1 93  ? 18.208 -47.106 30.382  1.00 46.95  ? 786  THR   A CA  1 
ATOM   645  C  C   . THR   A 1 93  ? 16.824 -47.287 31.088  1.00 46.58  ? 786  THR   A C   1 
ATOM   646  O  O   . THR   A 1 93  ? 15.823 -46.881 30.494  1.00 46.81  ? 786  THR   A O   1 
ATOM   647  C  CB  . THR   A 1 93  ? 19.514 -47.171 31.232  1.00 48.89  ? 786  THR   A CB  1 
ATOM   648  O  OG1 . THR   A 1 93  ? 20.617 -47.175 30.333  1.00 50.59  ? 786  THR   A OG1 1 
ATOM   649  C  CG2 . THR   A 1 93  ? 19.618 -48.398 32.054  1.00 49.95  ? 786  THR   A CG2 1 
ATOM   650  N  N   . SER   A 1 94  ? 16.723 -47.890 32.295  1.00 46.20  ? 787  SER   A N   1 
ATOM   651  C  CA  . SER   A 1 94  ? 15.461 -47.880 33.055  1.00 46.31  ? 787  SER   A CA  1 
ATOM   652  C  C   . SER   A 1 94  ? 15.255 -46.417 33.612  1.00 46.25  ? 787  SER   A C   1 
ATOM   653  O  O   . SER   A 1 94  ? 14.137 -46.042 33.964  1.00 46.57  ? 787  SER   A O   1 
ATOM   654  C  CB  . SER   A 1 94  ? 15.502 -48.862 34.230  1.00 47.37  ? 787  SER   A CB  1 
ATOM   655  O  OG  . SER   A 1 94  ? 16.141 -50.090 33.933  1.00 49.76  ? 787  SER   A OG  1 
ATOM   656  N  N   . THR   A 1 95  ? 16.353 -45.619 33.698  1.00 45.40  ? 788  THR   A N   1 
ATOM   657  C  CA  . THR   A 1 95  ? 16.430 -44.259 34.180  1.00 45.14  ? 788  THR   A CA  1 
ATOM   658  C  C   . THR   A 1 95  ? 16.908 -43.327 33.051  1.00 44.50  ? 788  THR   A C   1 
ATOM   659  O  O   . THR   A 1 95  ? 17.483 -43.761 32.037  1.00 44.20  ? 788  THR   A O   1 
ATOM   660  C  CB  . THR   A 1 95  ? 17.431 -44.213 35.365  1.00 46.70  ? 788  THR   A CB  1 
ATOM   661  O  OG1 . THR   A 1 95  ? 18.714 -44.671 34.933  1.00 47.88  ? 788  THR   A OG1 1 
ATOM   662  C  CG2 . THR   A 1 95  ? 16.993 -45.033 36.553  1.00 47.24  ? 788  THR   A CG2 1 
ATOM   663  N  N   . VAL   A 1 96  ? 16.680 -42.024 33.248  1.00 43.76  ? 789  VAL   A N   1 
ATOM   664  C  CA  . VAL   A 1 96  ? 17.140 -40.998 32.333  1.00 42.85  ? 789  VAL   A CA  1 
ATOM   665  C  C   . VAL   A 1 96  ? 18.479 -40.514 32.900  1.00 43.16  ? 789  VAL   A C   1 
ATOM   666  O  O   . VAL   A 1 96  ? 18.564 -40.170 34.085  1.00 43.16  ? 789  VAL   A O   1 
ATOM   667  C  CB  . VAL   A 1 96  ? 16.113 -39.841 32.231  1.00 42.22  ? 789  VAL   A CB  1 
ATOM   668  C  CG1 . VAL   A 1 96  ? 16.705 -38.640 31.508  1.00 42.23  ? 789  VAL   A CG1 1 
ATOM   669  C  CG2 . VAL   A 1 96  ? 14.832 -40.300 31.557  1.00 42.25  ? 789  VAL   A CG2 1 
ATOM   670  N  N   . GLN   A 1 97  ? 19.531 -40.524 32.074  1.00 43.03  ? 790  GLN   A N   1 
ATOM   671  C  CA  . GLN   A 1 97  ? 20.835 -40.050 32.518  1.00 43.32  ? 790  GLN   A CA  1 
ATOM   672  C  C   . GLN   A 1 97  ? 21.239 -38.832 31.710  1.00 43.42  ? 790  GLN   A C   1 
ATOM   673  O  O   . GLN   A 1 97  ? 21.348 -38.924 30.489  1.00 44.22  ? 790  GLN   A O   1 
ATOM   674  C  CB  . GLN   A 1 97  ? 21.880 -41.161 32.429  1.00 44.79  ? 790  GLN   A CB  1 
ATOM   675  C  CG  . GLN   A 1 97  ? 21.580 -42.280 33.407  1.00 47.71  ? 790  GLN   A CG  1 
ATOM   676  C  CD  . GLN   A 1 97  ? 22.767 -43.171 33.646  1.00 49.59  ? 790  GLN   A CD  1 
ATOM   677  O  OE1 . GLN   A 1 97  ? 23.649 -42.870 34.453  1.00 50.83  ? 790  GLN   A OE1 1 
ATOM   678  N  NE2 . GLN   A 1 97  ? 22.796 -44.291 32.950  1.00 48.53  ? 790  GLN   A NE2 1 
ATOM   679  N  N   . LEU   A 1 98  ? 21.402 -37.676 32.375  1.00 42.35  ? 791  LEU   A N   1 
ATOM   680  C  CA  . LEU   A 1 98  ? 21.763 -36.418 31.723  1.00 41.99  ? 791  LEU   A CA  1 
ATOM   681  C  C   . LEU   A 1 98  ? 23.241 -36.147 31.935  1.00 42.37  ? 791  LEU   A C   1 
ATOM   682  O  O   . LEU   A 1 98  ? 23.721 -36.230 33.053  1.00 42.70  ? 791  LEU   A O   1 
ATOM   683  C  CB  . LEU   A 1 98  ? 20.915 -35.281 32.294  1.00 41.81  ? 791  LEU   A CB  1 
ATOM   684  C  CG  . LEU   A 1 98  ? 19.423 -35.470 32.132  1.00 42.88  ? 791  LEU   A CG  1 
ATOM   685  C  CD1 . LEU   A 1 98  ? 18.662 -34.426 32.887  1.00 43.04  ? 791  LEU   A CD1 1 
ATOM   686  C  CD2 . LEU   A 1 98  ? 19.015 -35.481 30.669  1.00 43.56  ? 791  LEU   A CD2 1 
ATOM   687  N  N   . ILE   A 1 99  ? 23.969 -35.847 30.868  1.00 42.54  ? 792  ILE   A N   1 
ATOM   688  C  CA  . ILE   A 1 99  ? 25.414 -35.652 30.936  1.00 43.24  ? 792  ILE   A CA  1 
ATOM   689  C  C   . ILE   A 1 99  ? 25.806 -34.205 30.638  1.00 44.00  ? 792  ILE   A C   1 
ATOM   690  O  O   . ILE   A 1 99  ? 25.273 -33.601 29.722  1.00 43.68  ? 792  ILE   A O   1 
ATOM   691  C  CB  . ILE   A 1 99  ? 26.128 -36.686 29.999  1.00 43.35  ? 792  ILE   A CB  1 
ATOM   692  C  CG1 . ILE   A 1 99  ? 25.921 -38.146 30.490  1.00 43.69  ? 792  ILE   A CG1 1 
ATOM   693  C  CG2 . ILE   A 1 99  ? 27.608 -36.376 29.847  1.00 43.69  ? 792  ILE   A CG2 1 
ATOM   694  C  CD1 . ILE   A 1 99  ? 24.795 -38.913 29.846  1.00 44.66  ? 792  ILE   A CD1 1 
ATOM   695  N  N   . THR   A 1 100 ? 26.702 -33.641 31.440  1.00 45.15  ? 793  THR   A N   1 
ATOM   696  C  CA  . THR   A 1 100 ? 27.163 -32.266 31.258  1.00 47.14  ? 793  THR   A CA  1 
ATOM   697  C  C   . THR   A 1 100 ? 28.636 -32.119 31.688  1.00 49.28  ? 793  THR   A C   1 
ATOM   698  O  O   . THR   A 1 100 ? 29.187 -33.035 32.296  1.00 49.53  ? 793  THR   A O   1 
ATOM   699  C  CB  . THR   A 1 100 ? 26.232 -31.279 32.003  1.00 48.22  ? 793  THR   A CB  1 
ATOM   700  O  OG1 . THR   A 1 100 ? 26.317 -30.006 31.370  1.00 48.65  ? 793  THR   A OG1 1 
ATOM   701  C  CG2 . THR   A 1 100 ? 26.574 -31.142 33.488  1.00 48.60  ? 793  THR   A CG2 1 
ATOM   702  N  N   . GLN   A 1 101 ? 29.279 -30.984 31.367  1.00 50.69  ? 794  GLN   A N   1 
ATOM   703  C  CA  . GLN   A 1 101 ? 30.664 -30.759 31.782  1.00 52.74  ? 794  GLN   A CA  1 
ATOM   704  C  C   . GLN   A 1 101 ? 30.741 -30.674 33.323  1.00 53.11  ? 794  GLN   A C   1 
ATOM   705  O  O   . GLN   A 1 101 ? 29.838 -30.129 33.961  1.00 52.97  ? 794  GLN   A O   1 
ATOM   706  C  CB  . GLN   A 1 101 ? 31.220 -29.480 31.138  1.00 56.41  ? 794  GLN   A CB  1 
ATOM   707  C  CG  . GLN   A 1 101 ? 32.748 -29.424 31.120  1.00 63.91  ? 794  GLN   A CG  1 
ATOM   708  C  CD  . GLN   A 1 101 ? 33.276 -28.009 31.230  1.00 72.83  ? 794  GLN   A CD  1 
ATOM   709  O  OE1 . GLN   A 1 101 ? 32.702 -27.046 30.672  1.00 75.98  ? 794  GLN   A OE1 1 
ATOM   710  N  NE2 . GLN   A 1 101 ? 34.390 -27.849 31.959  1.00 73.91  ? 794  GLN   A NE2 1 
ATOM   711  N  N   . LEU   A 1 102 ? 31.791 -31.246 33.913  1.00 53.43  ? 795  LEU   A N   1 
ATOM   712  C  CA  . LEU   A 1 102 ? 31.955 -31.230 35.358  1.00 54.32  ? 795  LEU   A CA  1 
ATOM   713  C  C   . LEU   A 1 102 ? 32.315 -29.841 35.880  1.00 54.99  ? 795  LEU   A C   1 
ATOM   714  O  O   . LEU   A 1 102 ? 33.272 -29.233 35.405  1.00 54.95  ? 795  LEU   A O   1 
ATOM   715  C  CB  . LEU   A 1 102 ? 33.014 -32.266 35.775  1.00 54.65  ? 795  LEU   A CB  1 
ATOM   716  C  CG  . LEU   A 1 102 ? 33.131 -32.567 37.277  1.00 55.86  ? 795  LEU   A CG  1 
ATOM   717  C  CD1 . LEU   A 1 102 ? 31.815 -33.066 37.853  1.00 56.24  ? 795  LEU   A CD1 1 
ATOM   718  C  CD2 . LEU   A 1 102 ? 34.225 -33.573 37.543  1.00 56.41  ? 795  LEU   A CD2 1 
ATOM   719  N  N   . MET   A 1 103 ? 31.502 -29.334 36.835  1.00 55.55  ? 796  MET   A N   1 
ATOM   720  C  CA  . MET   A 1 103 ? 31.652 -28.057 37.549  1.00 56.44  ? 796  MET   A CA  1 
ATOM   721  C  C   . MET   A 1 103 ? 32.194 -28.472 38.901  1.00 57.08  ? 796  MET   A C   1 
ATOM   722  O  O   . MET   A 1 103 ? 31.498 -29.140 39.665  1.00 57.29  ? 796  MET   A O   1 
ATOM   723  C  CB  . MET   A 1 103 ? 30.296 -27.370 37.778  1.00 57.40  ? 796  MET   A CB  1 
ATOM   724  C  CG  . MET   A 1 103 ? 29.422 -27.304 36.557  1.00 58.95  ? 796  MET   A CG  1 
ATOM   725  S  SD  . MET   A 1 103 ? 29.831 -25.990 35.430  1.00 60.37  ? 796  MET   A SD  1 
ATOM   726  C  CE  . MET   A 1 103 ? 29.060 -26.625 34.001  1.00 61.82  ? 796  MET   A CE  1 
ATOM   727  N  N   . PRO   A 1 104 ? 33.444 -28.128 39.203  1.00 57.34  ? 797  PRO   A N   1 
ATOM   728  C  CA  . PRO   A 1 104 ? 34.068 -28.652 40.429  1.00 57.12  ? 797  PRO   A CA  1 
ATOM   729  C  C   . PRO   A 1 104 ? 33.559 -28.085 41.758  1.00 56.49  ? 797  PRO   A C   1 
ATOM   730  O  O   . PRO   A 1 104 ? 33.692 -28.741 42.792  1.00 56.90  ? 797  PRO   A O   1 
ATOM   731  C  CB  . PRO   A 1 104 ? 35.560 -28.351 40.228  1.00 58.19  ? 797  PRO   A CB  1 
ATOM   732  C  CG  . PRO   A 1 104 ? 35.712 -27.897 38.793  1.00 58.91  ? 797  PRO   A CG  1 
ATOM   733  C  CD  . PRO   A 1 104 ? 34.393 -27.351 38.382  1.00 57.22  ? 797  PRO   A CD  1 
ATOM   734  N  N   . PHE   A 1 105 ? 32.974 -26.885 41.742  1.00 55.05  ? 798  PHE   A N   1 
ATOM   735  C  CA  . PHE   A 1 105 ? 32.514 -26.244 42.970  1.00 53.69  ? 798  PHE   A CA  1 
ATOM   736  C  C   . PHE   A 1 105 ? 31.080 -26.570 43.399  1.00 52.36  ? 798  PHE   A C   1 
ATOM   737  O  O   . PHE   A 1 105 ? 30.629 -26.068 44.437  1.00 52.89  ? 798  PHE   A O   1 
ATOM   738  C  CB  . PHE   A 1 105 ? 32.697 -24.735 42.868  1.00 53.34  ? 798  PHE   A CB  1 
ATOM   739  C  CG  . PHE   A 1 105 ? 34.144 -24.348 42.732  1.00 53.52  ? 798  PHE   A CG  1 
ATOM   740  C  CD1 . PHE   A 1 105 ? 34.933 -24.155 43.850  1.00 54.07  ? 798  PHE   A CD1 1 
ATOM   741  C  CD2 . PHE   A 1 105 ? 34.721 -24.195 41.486  1.00 54.03  ? 798  PHE   A CD2 1 
ATOM   742  C  CE1 . PHE   A 1 105 ? 36.266 -23.794 43.721  1.00 54.53  ? 798  PHE   A CE1 1 
ATOM   743  C  CE2 . PHE   A 1 105 ? 36.055 -23.838 41.362  1.00 54.56  ? 798  PHE   A CE2 1 
ATOM   744  C  CZ  . PHE   A 1 105 ? 36.819 -23.642 42.479  1.00 54.20  ? 798  PHE   A CZ  1 
ATOM   745  N  N   . GLY   A 1 106 ? 30.398 -27.425 42.654  1.00 50.57  ? 799  GLY   A N   1 
ATOM   746  C  CA  . GLY   A 1 106 ? 29.027 -27.783 42.980  1.00 49.55  ? 799  GLY   A CA  1 
ATOM   747  C  C   . GLY   A 1 106 ? 28.098 -26.629 42.699  1.00 48.26  ? 799  GLY   A C   1 
ATOM   748  O  O   . GLY   A 1 106 ? 28.339 -25.875 41.758  1.00 48.82  ? 799  GLY   A O   1 
ATOM   749  N  N   . CYS   A 1 107 ? 27.057 -26.447 43.522  1.00 46.69  ? 800  CYS   A N   1 
ATOM   750  C  CA  . CYS   A 1 107 ? 26.103 -25.361 43.310  1.00 45.59  ? 800  CYS   A CA  1 
ATOM   751  C  C   . CYS   A 1 107 ? 26.372 -24.172 44.196  1.00 45.38  ? 800  CYS   A C   1 
ATOM   752  O  O   . CYS   A 1 107 ? 27.050 -24.285 45.220  1.00 46.12  ? 800  CYS   A O   1 
ATOM   753  C  CB  . CYS   A 1 107 ? 24.658 -25.842 43.426  1.00 45.45  ? 800  CYS   A CB  1 
ATOM   754  S  SG  . CYS   A 1 107 ? 24.199 -26.457 45.067  1.00 47.30  ? 800  CYS   A SG  1 
ATOM   755  N  N   . LEU   A 1 108 ? 25.862 -23.009 43.774  1.00 44.31  ? 801  LEU   A N   1 
ATOM   756  C  CA  . LEU   A 1 108 ? 26.029 -21.740 44.454  1.00 43.45  ? 801  LEU   A CA  1 
ATOM   757  C  C   . LEU   A 1 108 ? 25.370 -21.730 45.823  1.00 43.89  ? 801  LEU   A C   1 
ATOM   758  O  O   . LEU   A 1 108 ? 25.883 -21.058 46.706  1.00 44.22  ? 801  LEU   A O   1 
ATOM   759  C  CB  . LEU   A 1 108 ? 25.530 -20.596 43.555  1.00 42.47  ? 801  LEU   A CB  1 
ATOM   760  C  CG  . LEU   A 1 108 ? 25.980 -19.185 43.869  1.00 41.78  ? 801  LEU   A CG  1 
ATOM   761  C  CD1 . LEU   A 1 108 ? 27.489 -19.080 44.011  1.00 41.65  ? 801  LEU   A CD1 1 
ATOM   762  C  CD2 . LEU   A 1 108 ? 25.493 -18.243 42.804  1.00 42.24  ? 801  LEU   A CD2 1 
ATOM   763  N  N   . LEU   A 1 109 ? 24.316 -22.538 46.053  1.00 43.81  ? 802  LEU   A N   1 
ATOM   764  C  CA  . LEU   A 1 109 ? 23.690 -22.602 47.375  1.00 44.61  ? 802  LEU   A CA  1 
ATOM   765  C  C   . LEU   A 1 109 ? 24.710 -23.093 48.426  1.00 45.91  ? 802  LEU   A C   1 
ATOM   766  O  O   . LEU   A 1 109 ? 24.940 -22.410 49.429  1.00 46.55  ? 802  LEU   A O   1 
ATOM   767  C  CB  . LEU   A 1 109 ? 22.465 -23.540 47.360  1.00 44.54  ? 802  LEU   A CB  1 
ATOM   768  C  CG  . LEU   A 1 109 ? 21.220 -23.195 48.228  1.00 45.20  ? 802  LEU   A CG  1 
ATOM   769  C  CD1 . LEU   A 1 109 ? 20.514 -24.447 48.684  1.00 44.84  ? 802  LEU   A CD1 1 
ATOM   770  C  CD2 . LEU   A 1 109 ? 21.519 -22.266 49.423  1.00 45.69  ? 802  LEU   A CD2 1 
ATOM   771  N  N   . ASP   A 1 110 ? 25.358 -24.246 48.158  1.00 45.84  ? 803  ASP   A N   1 
ATOM   772  C  CA  . ASP   A 1 110 ? 26.369 -24.815 49.041  1.00 45.53  ? 803  ASP   A CA  1 
ATOM   773  C  C   . ASP   A 1 110 ? 27.615 -23.937 49.056  1.00 45.48  ? 803  ASP   A C   1 
ATOM   774  O  O   . ASP   A 1 110 ? 28.207 -23.758 50.113  1.00 45.29  ? 803  ASP   A O   1 
ATOM   775  C  CB  . ASP   A 1 110 ? 26.737 -26.229 48.584  1.00 46.54  ? 803  ASP   A CB  1 
ATOM   776  C  CG  . ASP   A 1 110 ? 25.558 -27.173 48.529  1.00 49.98  ? 803  ASP   A CG  1 
ATOM   777  O  OD1 . ASP   A 1 110 ? 24.595 -26.969 49.305  1.00 50.18  ? 803  ASP   A OD1 1 
ATOM   778  O  OD2 . ASP   A 1 110 ? 25.598 -28.122 47.713  1.00 52.51  ? 803  ASP   A OD2 1 
ATOM   779  N  N   . TYR   A 1 111 ? 27.999 -23.369 47.899  1.00 45.50  ? 804  TYR   A N   1 
ATOM   780  C  CA  . TYR   A 1 111 ? 29.173 -22.506 47.815  1.00 46.08  ? 804  TYR   A CA  1 
ATOM   781  C  C   . TYR   A 1 111 ? 29.058 -21.297 48.742  1.00 45.94  ? 804  TYR   A C   1 
ATOM   782  O  O   . TYR   A 1 111 ? 29.962 -21.066 49.538  1.00 46.00  ? 804  TYR   A O   1 
ATOM   783  C  CB  . TYR   A 1 111 ? 29.487 -22.086 46.359  1.00 46.52  ? 804  TYR   A CB  1 
ATOM   784  C  CG  . TYR   A 1 111 ? 30.794 -21.332 46.241  1.00 47.86  ? 804  TYR   A CG  1 
ATOM   785  C  CD1 . TYR   A 1 111 ? 30.848 -19.958 46.437  1.00 48.92  ? 804  TYR   A CD1 1 
ATOM   786  C  CD2 . TYR   A 1 111 ? 31.979 -21.994 45.957  1.00 49.03  ? 804  TYR   A CD2 1 
ATOM   787  C  CE1 . TYR   A 1 111 ? 32.053 -19.271 46.401  1.00 50.00  ? 804  TYR   A CE1 1 
ATOM   788  C  CE2 . TYR   A 1 111 ? 33.188 -21.312 45.884  1.00 50.12  ? 804  TYR   A CE2 1 
ATOM   789  C  CZ  . TYR   A 1 111 ? 33.223 -19.951 46.119  1.00 51.24  ? 804  TYR   A CZ  1 
ATOM   790  O  OH  . TYR   A 1 111 ? 34.415 -19.272 46.046  1.00 53.38  ? 804  TYR   A OH  1 
ATOM   791  N  N   . VAL   A 1 112 ? 27.950 -20.543 48.669  1.00 45.67  ? 805  VAL   A N   1 
ATOM   792  C  CA  . VAL   A 1 112 ? 27.777 -19.370 49.534  1.00 45.51  ? 805  VAL   A CA  1 
ATOM   793  C  C   . VAL   A 1 112 ? 27.644 -19.760 51.022  1.00 46.06  ? 805  VAL   A C   1 
ATOM   794  O  O   . VAL   A 1 112 ? 27.986 -18.956 51.892  1.00 46.46  ? 805  VAL   A O   1 
ATOM   795  C  CB  . VAL   A 1 112 ? 26.654 -18.397 49.082  1.00 44.96  ? 805  VAL   A CB  1 
ATOM   796  C  CG1 . VAL   A 1 112 ? 26.862 -17.943 47.646  1.00 45.08  ? 805  VAL   A CG1 1 
ATOM   797  C  CG2 . VAL   A 1 112 ? 25.268 -18.992 49.281  1.00 44.87  ? 805  VAL   A CG2 1 
ATOM   798  N  N   . ARG   A 1 113 ? 27.184 -20.982 51.316  1.00 45.97  ? 806  ARG   A N   1 
ATOM   799  C  CA  . ARG   A 1 113 ? 27.074 -21.435 52.698  1.00 46.64  ? 806  ARG   A CA  1 
ATOM   800  C  C   . ARG   A 1 113 ? 28.461 -21.780 53.257  1.00 48.86  ? 806  ARG   A C   1 
ATOM   801  O  O   . ARG   A 1 113 ? 28.783 -21.416 54.391  1.00 49.38  ? 806  ARG   A O   1 
ATOM   802  C  CB  . ARG   A 1 113 ? 26.162 -22.656 52.794  1.00 45.53  ? 806  ARG   A CB  1 
ATOM   803  C  CG  . ARG   A 1 113 ? 24.693 -22.332 52.834  1.00 44.05  ? 806  ARG   A CG  1 
ATOM   804  C  CD  . ARG   A 1 113 ? 23.912 -23.619 52.762  1.00 42.83  ? 806  ARG   A CD  1 
ATOM   805  N  NE  . ARG   A 1 113 ? 22.474 -23.386 52.782  1.00 42.80  ? 806  ARG   A NE  1 
ATOM   806  C  CZ  . ARG   A 1 113 ? 21.562 -24.307 52.500  1.00 45.04  ? 806  ARG   A CZ  1 
ATOM   807  N  NH1 . ARG   A 1 113 ? 21.933 -25.538 52.164  1.00 44.74  ? 806  ARG   A NH1 1 
ATOM   808  N  NH2 . ARG   A 1 113 ? 20.268 -24.005 52.551  1.00 45.69  ? 806  ARG   A NH2 1 
ATOM   809  N  N   . GLU   A 1 114 ? 29.283 -22.478 52.465  1.00 49.88  ? 807  GLU   A N   1 
ATOM   810  C  CA  . GLU   A 1 114 ? 30.610 -22.890 52.909  1.00 51.21  ? 807  GLU   A CA  1 
ATOM   811  C  C   . GLU   A 1 114 ? 31.639 -21.769 52.895  1.00 51.70  ? 807  GLU   A C   1 
ATOM   812  O  O   . GLU   A 1 114 ? 32.585 -21.798 53.684  1.00 52.14  ? 807  GLU   A O   1 
ATOM   813  C  CB  . GLU   A 1 114 ? 31.088 -24.098 52.108  1.00 54.65  ? 807  GLU   A CB  1 
ATOM   814  C  CG  . GLU   A 1 114 ? 30.186 -25.294 52.335  1.00 63.26  ? 807  GLU   A CG  1 
ATOM   815  C  CD  . GLU   A 1 114 ? 30.437 -26.457 51.401  1.00 75.77  ? 807  GLU   A CD  1 
ATOM   816  O  OE1 . GLU   A 1 114 ? 31.569 -26.555 50.869  1.00 79.05  ? 807  GLU   A OE1 1 
ATOM   817  O  OE2 . GLU   A 1 114 ? 29.504 -27.272 51.204  1.00 79.70  ? 807  GLU   A OE2 1 
ATOM   818  N  N   . HIS   A 1 115 ? 31.450 -20.768 52.026  1.00 51.36  ? 808  HIS   A N   1 
ATOM   819  C  CA  . HIS   A 1 115 ? 32.379 -19.648 51.918  1.00 51.18  ? 808  HIS   A CA  1 
ATOM   820  C  C   . HIS   A 1 115 ? 31.813 -18.325 52.436  1.00 51.05  ? 808  HIS   A C   1 
ATOM   821  O  O   . HIS   A 1 115 ? 32.341 -17.282 52.086  1.00 50.75  ? 808  HIS   A O   1 
ATOM   822  C  CB  . HIS   A 1 115 ? 32.863 -19.509 50.470  1.00 51.47  ? 808  HIS   A CB  1 
ATOM   823  C  CG  . HIS   A 1 115 ? 33.496 -20.751 49.944  1.00 53.23  ? 808  HIS   A CG  1 
ATOM   824  N  ND1 . HIS   A 1 115 ? 32.741 -21.771 49.410  1.00 55.17  ? 808  HIS   A ND1 1 
ATOM   825  C  CD2 . HIS   A 1 115 ? 34.799 -21.100 49.902  1.00 54.37  ? 808  HIS   A CD2 1 
ATOM   826  C  CE1 . HIS   A 1 115 ? 33.605 -22.702 49.046  1.00 55.79  ? 808  HIS   A CE1 1 
ATOM   827  N  NE2 . HIS   A 1 115 ? 34.856 -22.339 49.324  1.00 55.64  ? 808  HIS   A NE2 1 
ATOM   828  N  N   . LYS   A 1 116 ? 30.777 -18.384 53.293  1.00 51.44  ? 809  LYS   A N   1 
ATOM   829  C  CA  . LYS   A 1 116 ? 30.048 -17.281 53.932  1.00 52.43  ? 809  LYS   A CA  1 
ATOM   830  C  C   . LYS   A 1 116 ? 30.923 -16.119 54.434  1.00 53.33  ? 809  LYS   A C   1 
ATOM   831  O  O   . LYS   A 1 116 ? 30.593 -14.950 54.234  1.00 53.17  ? 809  LYS   A O   1 
ATOM   832  C  CB  . LYS   A 1 116 ? 29.201 -17.851 55.096  1.00 54.22  ? 809  LYS   A CB  1 
ATOM   833  C  CG  . LYS   A 1 116 ? 28.316 -16.829 55.779  1.00 58.94  ? 809  LYS   A CG  1 
ATOM   834  C  CD  . LYS   A 1 116 ? 28.695 -16.579 57.231  1.00 63.25  ? 809  LYS   A CD  1 
ATOM   835  C  CE  . LYS   A 1 116 ? 27.973 -15.373 57.819  1.00 65.43  ? 809  LYS   A CE  1 
ATOM   836  N  NZ  . LYS   A 1 116 ? 28.372 -14.100 57.162  1.00 66.56  ? 809  LYS   A NZ  1 
ATOM   837  N  N   . ASP   A 1 117 ? 32.028 -16.440 55.098  1.00 54.27  ? 810  ASP   A N   1 
ATOM   838  C  CA  . ASP   A 1 117 ? 32.920 -15.420 55.652  1.00 55.21  ? 810  ASP   A CA  1 
ATOM   839  C  C   . ASP   A 1 117 ? 34.057 -15.000 54.713  1.00 55.02  ? 810  ASP   A C   1 
ATOM   840  O  O   . ASP   A 1 117 ? 35.006 -14.354 55.147  1.00 55.15  ? 810  ASP   A O   1 
ATOM   841  C  CB  . ASP   A 1 117 ? 33.474 -15.890 57.006  1.00 57.73  ? 810  ASP   A CB  1 
ATOM   842  C  CG  . ASP   A 1 117 ? 32.400 -16.020 58.078  1.00 63.26  ? 810  ASP   A CG  1 
ATOM   843  O  OD1 . ASP   A 1 117 ? 31.746 -14.989 58.397  1.00 63.59  ? 810  ASP   A OD1 1 
ATOM   844  O  OD2 . ASP   A 1 117 ? 32.215 -17.150 58.603  1.00 65.90  ? 810  ASP   A OD2 1 
ATOM   845  N  N   . ASN   A 1 118 ? 33.942 -15.322 53.431  1.00 54.48  ? 811  ASN   A N   1 
ATOM   846  C  CA  . ASN   A 1 118 ? 34.959 -14.999 52.436  1.00 54.60  ? 811  ASN   A CA  1 
ATOM   847  C  C   . ASN   A 1 118 ? 34.418 -14.368 51.159  1.00 53.95  ? 811  ASN   A C   1 
ATOM   848  O  O   . ASN   A 1 118 ? 35.193 -14.100 50.240  1.00 54.09  ? 811  ASN   A O   1 
ATOM   849  C  CB  . ASN   A 1 118 ? 35.730 -16.264 52.081  1.00 56.15  ? 811  ASN   A CB  1 
ATOM   850  C  CG  . ASN   A 1 118 ? 36.799 -16.548 53.085  1.00 59.40  ? 811  ASN   A CG  1 
ATOM   851  O  OD1 . ASN   A 1 118 ? 36.699 -17.479 53.904  1.00 60.23  ? 811  ASN   A OD1 1 
ATOM   852  N  ND2 . ASN   A 1 118 ? 37.820 -15.696 53.062  1.00 60.02  ? 811  ASN   A ND2 1 
ATOM   853  N  N   . ILE   A 1 119 ? 33.098 -14.155 51.086  1.00 53.13  ? 812  ILE   A N   1 
ATOM   854  C  CA  . ILE   A 1 119 ? 32.438 -13.611 49.909  1.00 52.75  ? 812  ILE   A CA  1 
ATOM   855  C  C   . ILE   A 1 119 ? 32.235 -12.107 50.066  1.00 53.26  ? 812  ILE   A C   1 
ATOM   856  O  O   . ILE   A 1 119 ? 31.716 -11.656 51.081  1.00 53.61  ? 812  ILE   A O   1 
ATOM   857  C  CB  . ILE   A 1 119 ? 31.123 -14.382 49.630  1.00 52.17  ? 812  ILE   A CB  1 
ATOM   858  C  CG1 . ILE   A 1 119 ? 31.419 -15.845 49.310  1.00 52.46  ? 812  ILE   A CG1 1 
ATOM   859  C  CG2 . ILE   A 1 119 ? 30.356 -13.743 48.498  1.00 52.43  ? 812  ILE   A CG2 1 
ATOM   860  C  CD1 . ILE   A 1 119 ? 30.250 -16.708 49.332  1.00 53.31  ? 812  ILE   A CD1 1 
ATOM   861  N  N   . GLY   A 1 120 ? 32.703 -11.343 49.088  1.00 53.24  ? 813  GLY   A N   1 
ATOM   862  C  CA  . GLY   A 1 120 ? 32.593 -9.896  49.106  1.00 53.77  ? 813  GLY   A CA  1 
ATOM   863  C  C   . GLY   A 1 120 ? 31.450 -9.375  48.260  1.00 54.15  ? 813  GLY   A C   1 
ATOM   864  O  O   . GLY   A 1 120 ? 30.716 -10.148 47.640  1.00 54.78  ? 813  GLY   A O   1 
ATOM   865  N  N   . SER   A 1 121 ? 31.289 -8.046  48.229  1.00 53.42  ? 814  SER   A N   1 
ATOM   866  C  CA  . SER   A 1 121 ? 30.221 -7.405  47.472  1.00 52.48  ? 814  SER   A CA  1 
ATOM   867  C  C   . SER   A 1 121 ? 30.413 -7.518  45.981  1.00 51.52  ? 814  SER   A C   1 
ATOM   868  O  O   . SER   A 1 121 ? 29.425 -7.553  45.261  1.00 52.12  ? 814  SER   A O   1 
ATOM   869  C  CB  . SER   A 1 121 ? 30.076 -5.945  47.872  1.00 53.50  ? 814  SER   A CB  1 
ATOM   870  O  OG  . SER   A 1 121 ? 31.335 -5.298  47.961  1.00 55.94  ? 814  SER   A OG  1 
ATOM   871  N  N   . GLN   A 1 122 ? 31.667 -7.572  45.509  1.00 50.24  ? 815  GLN   A N   1 
ATOM   872  C  CA  . GLN   A 1 122 ? 31.987 -7.680  44.085  1.00 49.69  ? 815  GLN   A CA  1 
ATOM   873  C  C   . GLN   A 1 122 ? 31.523 -9.023  43.536  1.00 49.38  ? 815  GLN   A C   1 
ATOM   874  O  O   . GLN   A 1 122 ? 30.971 -9.070  42.450  1.00 49.51  ? 815  GLN   A O   1 
ATOM   875  C  CB  . GLN   A 1 122 ? 33.499 -7.481  43.851  1.00 50.76  ? 815  GLN   A CB  1 
ATOM   876  C  CG  . GLN   A 1 122 ? 33.947 -7.489  42.396  1.00 53.65  ? 815  GLN   A CG  1 
ATOM   877  C  CD  . GLN   A 1 122 ? 33.598 -6.210  41.656  1.00 58.96  ? 815  GLN   A CD  1 
ATOM   878  O  OE1 . GLN   A 1 122 ? 34.392 -5.262  41.584  1.00 61.00  ? 815  GLN   A OE1 1 
ATOM   879  N  NE2 . GLN   A 1 122 ? 32.408 -6.160  41.063  1.00 59.58  ? 815  GLN   A NE2 1 
ATOM   880  N  N   . TYR   A 1 123 ? 31.689 -10.103 44.309  1.00 48.99  ? 816  TYR   A N   1 
ATOM   881  C  CA  . TYR   A 1 123 ? 31.275 -11.441 43.895  1.00 48.90  ? 816  TYR   A CA  1 
ATOM   882  C  C   . TYR   A 1 123 ? 29.773 -11.609 43.875  1.00 47.11  ? 816  TYR   A C   1 
ATOM   883  O  O   . TYR   A 1 123 ? 29.238 -12.045 42.859  1.00 46.86  ? 816  TYR   A O   1 
ATOM   884  C  CB  . TYR   A 1 123 ? 31.942 -12.523 44.753  1.00 50.18  ? 816  TYR   A CB  1 
ATOM   885  C  CG  . TYR   A 1 123 ? 33.300 -12.905 44.220  1.00 52.64  ? 816  TYR   A CG  1 
ATOM   886  C  CD1 . TYR   A 1 123 ? 34.370 -12.022 44.287  1.00 54.33  ? 816  TYR   A CD1 1 
ATOM   887  C  CD2 . TYR   A 1 123 ? 33.504 -14.126 43.602  1.00 53.91  ? 816  TYR   A CD2 1 
ATOM   888  C  CE1 . TYR   A 1 123 ? 35.610 -12.349 43.765  1.00 55.60  ? 816  TYR   A CE1 1 
ATOM   889  C  CE2 . TYR   A 1 123 ? 34.741 -14.466 43.077  1.00 55.16  ? 816  TYR   A CE2 1 
ATOM   890  C  CZ  . TYR   A 1 123 ? 35.796 -13.580 43.175  1.00 56.73  ? 816  TYR   A CZ  1 
ATOM   891  O  OH  . TYR   A 1 123 ? 37.025 -13.897 42.658  1.00 59.27  ? 816  TYR   A OH  1 
ATOM   892  N  N   . LEU   A 1 124 ? 29.082 -11.241 44.973  1.00 45.56  ? 817  LEU   A N   1 
ATOM   893  C  CA  . LEU   A 1 124 ? 27.631 -11.357 45.051  1.00 44.68  ? 817  LEU   A CA  1 
ATOM   894  C  C   . LEU   A 1 124 ? 26.924 -10.596 43.919  1.00 44.22  ? 817  LEU   A C   1 
ATOM   895  O  O   . LEU   A 1 124 ? 26.092 -11.170 43.219  1.00 44.86  ? 817  LEU   A O   1 
ATOM   896  C  CB  . LEU   A 1 124 ? 27.133 -10.861 46.403  1.00 44.47  ? 817  LEU   A CB  1 
ATOM   897  C  CG  . LEU   A 1 124 ? 27.494 -11.694 47.602  1.00 45.22  ? 817  LEU   A CG  1 
ATOM   898  C  CD1 . LEU   A 1 124 ? 27.333 -10.891 48.861  1.00 45.68  ? 817  LEU   A CD1 1 
ATOM   899  C  CD2 . LEU   A 1 124 ? 26.645 -12.936 47.678  1.00 45.58  ? 817  LEU   A CD2 1 
ATOM   900  N  N   . LEU   A 1 125 ? 27.292 -9.335  43.707  1.00 43.05  ? 818  LEU   A N   1 
ATOM   901  C  CA  . LEU   A 1 125 ? 26.708 -8.504  42.664  1.00 42.53  ? 818  LEU   A CA  1 
ATOM   902  C  C   . LEU   A 1 125 ? 27.014 -9.043  41.272  1.00 42.77  ? 818  LEU   A C   1 
ATOM   903  O  O   . LEU   A 1 125 ? 26.144 -9.028  40.402  1.00 42.80  ? 818  LEU   A O   1 
ATOM   904  C  CB  . LEU   A 1 125 ? 27.168 -7.045  42.828  1.00 42.01  ? 818  LEU   A CB  1 
ATOM   905  C  CG  . LEU   A 1 125 ? 26.591 -6.340  44.060  1.00 42.59  ? 818  LEU   A CG  1 
ATOM   906  C  CD1 . LEU   A 1 125 ? 27.246 -5.002  44.285  1.00 42.85  ? 818  LEU   A CD1 1 
ATOM   907  C  CD2 . LEU   A 1 125 ? 25.091 -6.193  43.949  1.00 42.86  ? 818  LEU   A CD2 1 
ATOM   908  N  N   . ASN   A 1 126 ? 28.220 -9.582  41.074  1.00 42.81  ? 819  ASN   A N   1 
ATOM   909  C  CA  . ASN   A 1 126 ? 28.594 -10.159 39.786  1.00 43.08  ? 819  ASN   A CA  1 
ATOM   910  C  C   . ASN   A 1 126 ? 27.863 -11.453 39.502  1.00 42.58  ? 819  ASN   A C   1 
ATOM   911  O  O   . ASN   A 1 126 ? 27.605 -11.746 38.342  1.00 43.02  ? 819  ASN   A O   1 
ATOM   912  C  CB  . ASN   A 1 126 ? 30.094 -10.330 39.655  1.00 45.39  ? 819  ASN   A CB  1 
ATOM   913  C  CG  . ASN   A 1 126 ? 30.788 -9.108  39.105  1.00 51.96  ? 819  ASN   A CG  1 
ATOM   914  O  OD1 . ASN   A 1 126 ? 30.350 -8.481  38.126  1.00 54.81  ? 819  ASN   A OD1 1 
ATOM   915  N  ND2 . ASN   A 1 126 ? 31.894 -8.740  39.718  1.00 53.17  ? 819  ASN   A ND2 1 
ATOM   916  N  N   . TRP   A 1 127 ? 27.508 -12.223 40.538  1.00 41.84  ? 820  TRP   A N   1 
ATOM   917  C  CA  . TRP   A 1 127 ? 26.722 -13.438 40.343  1.00 41.48  ? 820  TRP   A CA  1 
ATOM   918  C  C   . TRP   A 1 127 ? 25.301 -13.055 39.919  1.00 40.46  ? 820  TRP   A C   1 
ATOM   919  O  O   . TRP   A 1 127 ? 24.735 -13.701 39.051  1.00 40.50  ? 820  TRP   A O   1 
ATOM   920  C  CB  . TRP   A 1 127 ? 26.714 -14.324 41.600  1.00 41.90  ? 820  TRP   A CB  1 
ATOM   921  C  CG  . TRP   A 1 127 ? 28.035 -14.967 41.909  1.00 43.13  ? 820  TRP   A CG  1 
ATOM   922  C  CD1 . TRP   A 1 127 ? 28.993 -15.352 41.015  1.00 44.25  ? 820  TRP   A CD1 1 
ATOM   923  C  CD2 . TRP   A 1 127 ? 28.529 -15.330 43.209  1.00 43.61  ? 820  TRP   A CD2 1 
ATOM   924  N  NE1 . TRP   A 1 127 ? 30.063 -15.907 41.680  1.00 44.87  ? 820  TRP   A NE1 1 
ATOM   925  C  CE2 . TRP   A 1 127 ? 29.803 -15.906 43.030  1.00 44.71  ? 820  TRP   A CE2 1 
ATOM   926  C  CE3 . TRP   A 1 127 ? 28.030 -15.201 44.511  1.00 44.24  ? 820  TRP   A CE3 1 
ATOM   927  C  CZ2 . TRP   A 1 127 ? 30.587 -16.337 44.107  1.00 45.27  ? 820  TRP   A CZ2 1 
ATOM   928  C  CZ3 . TRP   A 1 127 ? 28.805 -15.634 45.571  1.00 45.25  ? 820  TRP   A CZ3 1 
ATOM   929  C  CH2 . TRP   A 1 127 ? 30.068 -16.192 45.365  1.00 45.35  ? 820  TRP   A CH2 1 
ATOM   930  N  N   . CYS   A 1 128 ? 24.748 -11.969 40.478  1.00 39.52  ? 821  CYS   A N   1 
ATOM   931  C  CA  . CYS   A 1 128 ? 23.433 -11.473 40.110  1.00 38.80  ? 821  CYS   A CA  1 
ATOM   932  C  C   . CYS   A 1 128 ? 23.377 -11.074 38.632  1.00 38.38  ? 821  CYS   A C   1 
ATOM   933  O  O   . CYS   A 1 128 ? 22.358 -11.282 37.979  1.00 38.77  ? 821  CYS   A O   1 
ATOM   934  C  CB  . CYS   A 1 128 ? 23.030 -10.320 41.020  1.00 38.75  ? 821  CYS   A CB  1 
ATOM   935  S  SG  . CYS   A 1 128 ? 22.823 -10.792 42.756  1.00 40.51  ? 821  CYS   A SG  1 
ATOM   936  N  N   . VAL   A 1 129 ? 24.469 -10.527 38.101  1.00 37.47  ? 822  VAL   A N   1 
ATOM   937  C  CA  . VAL   A 1 129 ? 24.542 -10.163 36.689  1.00 37.13  ? 822  VAL   A CA  1 
ATOM   938  C  C   . VAL   A 1 129 ? 24.565 -11.421 35.828  1.00 37.30  ? 822  VAL   A C   1 
ATOM   939  O  O   . VAL   A 1 129 ? 23.791 -11.521 34.887  1.00 38.26  ? 822  VAL   A O   1 
ATOM   940  C  CB  . VAL   A 1 129 ? 25.774 -9.281  36.382  1.00 37.32  ? 822  VAL   A CB  1 
ATOM   941  C  CG1 . VAL   A 1 129 ? 25.852 -8.973  34.901  1.00 37.83  ? 822  VAL   A CG1 1 
ATOM   942  C  CG2 . VAL   A 1 129 ? 25.745 -7.999  37.198  1.00 37.58  ? 822  VAL   A CG2 1 
ATOM   943  N  N   . GLN   A 1 130 ? 25.426 -12.393 36.157  1.00 36.12  ? 823  GLN   A N   1 
ATOM   944  C  CA  . GLN   A 1 130 ? 25.541 -13.634 35.396  1.00 35.49  ? 823  GLN   A CA  1 
ATOM   945  C  C   . GLN   A 1 130 ? 24.243 -14.439 35.354  1.00 35.80  ? 823  GLN   A C   1 
ATOM   946  O  O   . GLN   A 1 130 ? 23.834 -14.854 34.279  1.00 36.49  ? 823  GLN   A O   1 
ATOM   947  C  CB  . GLN   A 1 130 ? 26.708 -14.476 35.916  1.00 35.89  ? 823  GLN   A CB  1 
ATOM   948  C  CG  . GLN   A 1 130 ? 28.028 -13.725 35.834  1.00 37.38  ? 823  GLN   A CG  1 
ATOM   949  C  CD  . GLN   A 1 130 ? 29.235 -14.542 36.212  1.00 39.72  ? 823  GLN   A CD  1 
ATOM   950  O  OE1 . GLN   A 1 130 ? 29.162 -15.746 36.455  1.00 39.45  ? 823  GLN   A OE1 1 
ATOM   951  N  NE2 . GLN   A 1 130 ? 30.387 -13.895 36.261  1.00 40.51  ? 823  GLN   A NE2 1 
ATOM   952  N  N   . ILE   A 1 131 ? 23.558 -14.602 36.485  1.00 35.40  ? 824  ILE   A N   1 
ATOM   953  C  CA  . ILE   A 1 131 ? 22.277 -15.305 36.522  1.00 35.53  ? 824  ILE   A CA  1 
ATOM   954  C  C   . ILE   A 1 131 ? 21.223 -14.584 35.675  1.00 36.19  ? 824  ILE   A C   1 
ATOM   955  O  O   . ILE   A 1 131 ? 20.480 -15.231 34.943  1.00 36.48  ? 824  ILE   A O   1 
ATOM   956  C  CB  . ILE   A 1 131 ? 21.803 -15.511 37.977  1.00 35.51  ? 824  ILE   A CB  1 
ATOM   957  C  CG1 . ILE   A 1 131 ? 22.864 -16.293 38.800  1.00 35.69  ? 824  ILE   A CG1 1 
ATOM   958  C  CG2 . ILE   A 1 131 ? 20.438 -16.206 37.998  1.00 35.59  ? 824  ILE   A CG2 1 
ATOM   959  C  CD1 . ILE   A 1 131 ? 22.690 -16.243 40.255  1.00 36.20  ? 824  ILE   A CD1 1 
ATOM   960  N  N   . ALA   A 1 132 ? 21.197 -13.243 35.718  1.00 36.30  ? 825  ALA   A N   1 
ATOM   961  C  CA  . ALA   A 1 132 ? 20.258 -12.455 34.912  1.00 36.90  ? 825  ALA   A CA  1 
ATOM   962  C  C   . ALA   A 1 132 ? 20.615 -12.507 33.409  1.00 37.96  ? 825  ALA   A C   1 
ATOM   963  O  O   . ALA   A 1 132 ? 19.723 -12.457 32.560  1.00 38.55  ? 825  ALA   A O   1 
ATOM   964  C  CB  . ALA   A 1 132 ? 20.226 -11.021 35.399  1.00 36.78  ? 825  ALA   A CB  1 
ATOM   965  N  N   . LYS   A 1 133 ? 21.917 -12.623 33.085  1.00 37.75  ? 826  LYS   A N   1 
ATOM   966  C  CA  . LYS   A 1 133 ? 22.415 -12.776 31.716  1.00 37.63  ? 826  LYS   A CA  1 
ATOM   967  C  C   . LYS   A 1 133 ? 21.980 -14.142 31.152  1.00 37.86  ? 826  LYS   A C   1 
ATOM   968  O  O   . LYS   A 1 133 ? 21.548 -14.230 30.002  1.00 38.24  ? 826  LYS   A O   1 
ATOM   969  C  CB  . LYS   A 1 133 ? 23.946 -12.652 31.687  1.00 38.63  ? 826  LYS   A CB  1 
ATOM   970  C  CG  . LYS   A 1 133 ? 24.457 -11.226 31.748  1.00 41.56  ? 826  LYS   A CG  1 
ATOM   971  C  CD  . LYS   A 1 133 ? 25.953 -11.197 31.802  1.00 46.42  ? 826  LYS   A CD  1 
ATOM   972  C  CE  . LYS   A 1 133 ? 26.492 -9.866  31.359  1.00 52.06  ? 826  LYS   A CE  1 
ATOM   973  N  NZ  . LYS   A 1 133 ? 27.946 -9.711  31.670  1.00 56.11  ? 826  LYS   A NZ  1 
ATOM   974  N  N   . GLY   A 1 134 ? 22.060 -15.176 31.982  1.00 37.79  ? 827  GLY   A N   1 
ATOM   975  C  CA  . GLY   A 1 134 ? 21.650 -16.518 31.599  1.00 38.51  ? 827  GLY   A CA  1 
ATOM   976  C  C   . GLY   A 1 134 ? 20.152 -16.633 31.410  1.00 38.52  ? 827  GLY   A C   1 
ATOM   977  O  O   . GLY   A 1 134 ? 19.696 -17.211 30.421  1.00 38.26  ? 827  GLY   A O   1 
ATOM   978  N  N   . MET   A 1 135 ? 19.375 -16.049 32.353  1.00 38.31  ? 828  MET   A N   1 
ATOM   979  C  CA  . MET   A 1 135 ? 17.914 -16.065 32.324  1.00 38.37  ? 828  MET   A CA  1 
ATOM   980  C  C   . MET   A 1 135 ? 17.345 -15.225 31.175  1.00 38.51  ? 828  MET   A C   1 
ATOM   981  O  O   . MET   A 1 135 ? 16.354 -15.601 30.551  1.00 38.02  ? 828  MET   A O   1 
ATOM   982  C  CB  . MET   A 1 135 ? 17.353 -15.607 33.668  1.00 38.80  ? 828  MET   A CB  1 
ATOM   983  C  CG  . MET   A 1 135 ? 17.540 -16.623 34.785  1.00 40.32  ? 828  MET   A CG  1 
ATOM   984  S  SD  . MET   A 1 135 ? 16.753 -18.217 34.459  1.00 41.24  ? 828  MET   A SD  1 
ATOM   985  C  CE  . MET   A 1 135 ? 15.088 -17.799 34.682  1.00 38.89  ? 828  MET   A CE  1 
ATOM   986  N  N   . ASN   A 1 136 ? 17.999 -14.103 30.874  1.00 38.79  ? 829  ASN   A N   1 
ATOM   987  C  CA  . ASN   A 1 136 ? 17.622 -13.237 29.767  1.00 39.28  ? 829  ASN   A CA  1 
ATOM   988  C  C   . ASN   A 1 136 ? 17.816 -14.014 28.448  1.00 39.73  ? 829  ASN   A C   1 
ATOM   989  O  O   . ASN   A 1 136 ? 16.974 -13.928 27.551  1.00 40.17  ? 829  ASN   A O   1 
ATOM   990  C  CB  . ASN   A 1 136 ? 18.487 -11.977 29.806  1.00 41.08  ? 829  ASN   A CB  1 
ATOM   991  C  CG  . ASN   A 1 136 ? 18.420 -11.097 28.586  1.00 44.87  ? 829  ASN   A CG  1 
ATOM   992  O  OD1 . ASN   A 1 136 ? 17.371 -10.525 28.265  1.00 46.67  ? 829  ASN   A OD1 1 
ATOM   993  N  ND2 . ASN   A 1 136 ? 19.548 -10.966 27.891  1.00 44.74  ? 829  ASN   A ND2 1 
ATOM   994  N  N   . TYR   A 1 137 ? 18.895 -14.811 28.348  1.00 39.34  ? 830  TYR   A N   1 
ATOM   995  C  CA  . TYR   A 1 137 ? 19.127 -15.636 27.171  1.00 39.03  ? 830  TYR   A CA  1 
ATOM   996  C  C   . TYR   A 1 137 ? 18.024 -16.699 27.046  1.00 39.49  ? 830  TYR   A C   1 
ATOM   997  O  O   . TYR   A 1 137 ? 17.541 -16.923 25.946  1.00 39.64  ? 830  TYR   A O   1 
ATOM   998  C  CB  . TYR   A 1 137 ? 20.517 -16.277 27.213  1.00 38.58  ? 830  TYR   A CB  1 
ATOM   999  C  CG  . TYR   A 1 137 ? 20.715 -17.289 26.107  1.00 38.90  ? 830  TYR   A CG  1 
ATOM   1000 C  CD1 . TYR   A 1 137 ? 20.885 -16.887 24.792  1.00 39.91  ? 830  TYR   A CD1 1 
ATOM   1001 C  CD2 . TYR   A 1 137 ? 20.656 -18.646 26.365  1.00 39.25  ? 830  TYR   A CD2 1 
ATOM   1002 C  CE1 . TYR   A 1 137 ? 21.028 -17.810 23.770  1.00 40.34  ? 830  TYR   A CE1 1 
ATOM   1003 C  CE2 . TYR   A 1 137 ? 20.797 -19.574 25.354  1.00 40.18  ? 830  TYR   A CE2 1 
ATOM   1004 C  CZ  . TYR   A 1 137 ? 20.995 -19.153 24.061  1.00 41.05  ? 830  TYR   A CZ  1 
ATOM   1005 O  OH  . TYR   A 1 137 ? 21.098 -20.094 23.073  1.00 42.31  ? 830  TYR   A OH  1 
ATOM   1006 N  N   . LEU   A 1 138 ? 17.610 -17.339 28.156  1.00 39.89  ? 831  LEU   A N   1 
ATOM   1007 C  CA  . LEU   A 1 138 ? 16.525 -18.323 28.113  1.00 40.67  ? 831  LEU   A CA  1 
ATOM   1008 C  C   . LEU   A 1 138 ? 15.227 -17.660 27.663  1.00 42.26  ? 831  LEU   A C   1 
ATOM   1009 O  O   . LEU   A 1 138 ? 14.478 -18.271 26.912  1.00 42.58  ? 831  LEU   A O   1 
ATOM   1010 C  CB  . LEU   A 1 138 ? 16.307 -19.009 29.466  1.00 40.22  ? 831  LEU   A CB  1 
ATOM   1011 C  CG  . LEU   A 1 138 ? 17.417 -19.919 29.991  1.00 41.01  ? 831  LEU   A CG  1 
ATOM   1012 C  CD1 . LEU   A 1 138 ? 16.987 -20.600 31.263  1.00 41.21  ? 831  LEU   A CD1 1 
ATOM   1013 C  CD2 . LEU   A 1 138 ? 17.790 -20.984 28.997  1.00 41.59  ? 831  LEU   A CD2 1 
ATOM   1014 N  N   . GLU   A 1 139 ? 14.983 -16.396 28.084  1.00 43.05  ? 832  GLU   A N   1 
ATOM   1015 C  CA  . GLU   A 1 139 ? 13.814 -15.608 27.683  1.00 43.78  ? 832  GLU   A CA  1 
ATOM   1016 C  C   . GLU   A 1 139 ? 13.848 -15.375 26.168  1.00 45.29  ? 832  GLU   A C   1 
ATOM   1017 O  O   . GLU   A 1 139 ? 12.835 -15.559 25.488  1.00 45.35  ? 832  GLU   A O   1 
ATOM   1018 C  CB  . GLU   A 1 139 ? 13.759 -14.279 28.445  1.00 44.52  ? 832  GLU   A CB  1 
ATOM   1019 C  CG  . GLU   A 1 139 ? 12.624 -13.378 27.992  1.00 47.77  ? 832  GLU   A CG  1 
ATOM   1020 C  CD  . GLU   A 1 139 ? 12.170 -12.294 28.952  1.00 51.35  ? 832  GLU   A CD  1 
ATOM   1021 O  OE1 . GLU   A 1 139 ? 12.945 -11.920 29.863  1.00 52.32  ? 832  GLU   A OE1 1 
ATOM   1022 O  OE2 . GLU   A 1 139 ? 11.025 -11.816 28.785  1.00 52.40  ? 832  GLU   A OE2 1 
ATOM   1023 N  N   . ASP   A 1 140 ? 15.032 -15.042 25.633  1.00 46.28  ? 833  ASP   A N   1 
ATOM   1024 C  CA  . ASP   A 1 140 ? 15.263 -14.851 24.197  1.00 47.58  ? 833  ASP   A CA  1 
ATOM   1025 C  C   . ASP   A 1 140 ? 14.931 -16.142 23.421  1.00 48.84  ? 833  ASP   A C   1 
ATOM   1026 O  O   . ASP   A 1 140 ? 14.337 -16.105 22.335  1.00 49.85  ? 833  ASP   A O   1 
ATOM   1027 C  CB  . ASP   A 1 140 ? 16.729 -14.455 23.951  1.00 49.21  ? 833  ASP   A CB  1 
ATOM   1028 C  CG  . ASP   A 1 140 ? 17.064 -14.204 22.490  1.00 53.85  ? 833  ASP   A CG  1 
ATOM   1029 O  OD1 . ASP   A 1 140 ? 16.838 -13.072 22.017  1.00 53.87  ? 833  ASP   A OD1 1 
ATOM   1030 O  OD2 . ASP   A 1 140 ? 17.549 -15.148 21.816  1.00 56.73  ? 833  ASP   A OD2 1 
ATOM   1031 N  N   . ARG   A 1 141 ? 15.312 -17.283 23.992  1.00 48.50  ? 834  ARG   A N   1 
ATOM   1032 C  CA  . ARG   A 1 141 ? 15.050 -18.602 23.439  1.00 48.55  ? 834  ARG   A CA  1 
ATOM   1033 C  C   . ARG   A 1 141 ? 13.585 -19.072 23.639  1.00 49.14  ? 834  ARG   A C   1 
ATOM   1034 O  O   . ARG   A 1 141 ? 13.258 -20.201 23.272  1.00 49.29  ? 834  ARG   A O   1 
ATOM   1035 C  CB  . ARG   A 1 141 ? 16.021 -19.594 24.094  1.00 49.41  ? 834  ARG   A CB  1 
ATOM   1036 C  CG  . ARG   A 1 141 ? 17.058 -20.196 23.173  1.00 52.59  ? 834  ARG   A CG  1 
ATOM   1037 C  CD  . ARG   A 1 141 ? 17.853 -19.154 22.432  1.00 56.41  ? 834  ARG   A CD  1 
ATOM   1038 N  NE  . ARG   A 1 141 ? 17.799 -19.410 20.994  1.00 59.71  ? 834  ARG   A NE  1 
ATOM   1039 C  CZ  . ARG   A 1 141 ? 17.931 -18.476 20.059  1.00 62.10  ? 834  ARG   A CZ  1 
ATOM   1040 N  NH1 . ARG   A 1 141 ? 17.861 -18.800 18.777  1.00 61.78  ? 834  ARG   A NH1 1 
ATOM   1041 N  NH2 . ARG   A 1 141 ? 18.137 -17.208 20.401  1.00 62.20  ? 834  ARG   A NH2 1 
ATOM   1042 N  N   . ARG   A 1 142 ? 12.728 -18.213 24.251  1.00 49.34  ? 835  ARG   A N   1 
ATOM   1043 C  CA  . ARG   A 1 142 ? 11.318 -18.407 24.599  1.00 49.63  ? 835  ARG   A CA  1 
ATOM   1044 C  C   . ARG   A 1 142 ? 11.110 -19.579 25.544  1.00 48.66  ? 835  ARG   A C   1 
ATOM   1045 O  O   . ARG   A 1 142 ? 10.082 -20.240 25.488  1.00 49.11  ? 835  ARG   A O   1 
ATOM   1046 C  CB  . ARG   A 1 142 ? 10.434 -18.502 23.340  1.00 52.16  ? 835  ARG   A CB  1 
ATOM   1047 C  CG  . ARG   A 1 142 ? 10.305 -17.160 22.625  1.00 57.60  ? 835  ARG   A CG  1 
ATOM   1048 C  CD  . ARG   A 1 142 ? 9.584  -17.263 21.299  1.00 63.54  ? 835  ARG   A CD  1 
ATOM   1049 N  NE  . ARG   A 1 142 ? 10.326 -16.572 20.238  1.00 69.19  ? 835  ARG   A NE  1 
ATOM   1050 C  CZ  . ARG   A 1 142 ? 10.040 -16.660 18.941  1.00 72.68  ? 835  ARG   A CZ  1 
ATOM   1051 N  NH1 . ARG   A 1 142 ? 10.782 -16.019 18.047  1.00 72.74  ? 835  ARG   A NH1 1 
ATOM   1052 N  NH2 . ARG   A 1 142 ? 9.021  -17.407 18.526  1.00 72.99  ? 835  ARG   A NH2 1 
ATOM   1053 N  N   . LEU   A 1 143 ? 12.064 -19.808 26.438  1.00 47.54  ? 836  LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 143 ? 12.044 -20.926 27.377  1.00 47.27  ? 836  LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 143 ? 11.794 -20.454 28.791  1.00 46.13  ? 836  LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 143 ? 12.547 -19.625 29.288  1.00 46.80  ? 836  LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 143 ? 13.416 -21.634 27.326  1.00 47.84  ? 836  LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 143 ? 13.471 -23.108 27.694  1.00 49.52  ? 836  LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 143 ? 14.550 -23.794 26.926  1.00 50.21  ? 836  LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 143 ? 13.701 -23.311 29.181  1.00 50.28  ? 836  LEU   A CD2 1 
ATOM   1061 N  N   . VAL   A 1 144 ? 10.775 -21.006 29.462  1.00 44.53  ? 837  VAL   A N   1 
ATOM   1062 C  CA  . VAL   A 1 144 ? 10.499 -20.685 30.865  1.00 43.17  ? 837  VAL   A CA  1 
ATOM   1063 C  C   . VAL   A 1 144 ? 11.180 -21.785 31.695  1.00 43.14  ? 837  VAL   A C   1 
ATOM   1064 O  O   . VAL   A 1 144 ? 10.976 -22.968 31.412  1.00 43.89  ? 837  VAL   A O   1 
ATOM   1065 C  CB  . VAL   A 1 144 ? 8.987  -20.603 31.139  1.00 42.36  ? 837  VAL   A CB  1 
ATOM   1066 C  CG1 . VAL   A 1 144 ? 8.707  -20.342 32.612  1.00 42.36  ? 837  VAL   A CG1 1 
ATOM   1067 C  CG2 . VAL   A 1 144 ? 8.348  -19.540 30.272  1.00 42.50  ? 837  VAL   A CG2 1 
ATOM   1068 N  N   . HIS   A 1 145 ? 12.058 -21.416 32.644  1.00 42.06  ? 838  HIS   A N   1 
ATOM   1069 C  CA  . HIS   A 1 145 ? 12.798 -22.397 33.445  1.00 41.41  ? 838  HIS   A CA  1 
ATOM   1070 C  C   . HIS   A 1 145 ? 11.907 -23.156 34.443  1.00 41.68  ? 838  HIS   A C   1 
ATOM   1071 O  O   . HIS   A 1 145 ? 12.016 -24.382 34.533  1.00 42.17  ? 838  HIS   A O   1 
ATOM   1072 C  CB  . HIS   A 1 145 ? 13.969 -21.716 34.162  1.00 41.35  ? 838  HIS   A CB  1 
ATOM   1073 C  CG  . HIS   A 1 145 ? 14.929 -22.659 34.814  1.00 42.36  ? 838  HIS   A CG  1 
ATOM   1074 N  ND1 . HIS   A 1 145 ? 14.570 -23.408 35.911  1.00 43.53  ? 838  HIS   A ND1 1 
ATOM   1075 C  CD2 . HIS   A 1 145 ? 16.232 -22.890 34.540  1.00 43.27  ? 838  HIS   A CD2 1 
ATOM   1076 C  CE1 . HIS   A 1 145 ? 15.646 -24.093 36.250  1.00 43.77  ? 838  HIS   A CE1 1 
ATOM   1077 N  NE2 . HIS   A 1 145 ? 16.669 -23.819 35.452  1.00 43.90  ? 838  HIS   A NE2 1 
ATOM   1078 N  N   . ARG   A 1 146 ? 11.061 -22.420 35.216  1.00 41.22  ? 839  ARG   A N   1 
ATOM   1079 C  CA  . ARG   A 1 146 ? 10.117 -22.905 36.244  1.00 40.98  ? 839  ARG   A CA  1 
ATOM   1080 C  C   . ARG   A 1 146 ? 10.758 -23.277 37.564  1.00 40.57  ? 839  ARG   A C   1 
ATOM   1081 O  O   . ARG   A 1 146 ? 10.028 -23.491 38.537  1.00 41.15  ? 839  ARG   A O   1 
ATOM   1082 C  CB  . ARG   A 1 146 ? 9.284  -24.102 35.776  1.00 42.72  ? 839  ARG   A CB  1 
ATOM   1083 C  CG  . ARG   A 1 146 ? 8.337  -23.835 34.641  1.00 47.24  ? 839  ARG   A CG  1 
ATOM   1084 C  CD  . ARG   A 1 146 ? 7.763  -25.150 34.154  1.00 52.43  ? 839  ARG   A CD  1 
ATOM   1085 N  NE  . ARG   A 1 146 ? 6.536  -24.940 33.389  1.00 57.70  ? 839  ARG   A NE  1 
ATOM   1086 C  CZ  . ARG   A 1 146 ? 5.312  -25.184 33.849  1.00 60.90  ? 839  ARG   A CZ  1 
ATOM   1087 N  NH1 . ARG   A 1 146 ? 4.249  -24.929 33.093  1.00 61.31  ? 839  ARG   A NH1 1 
ATOM   1088 N  NH2 . ARG   A 1 146 ? 5.139  -25.660 35.079  1.00 60.35  ? 839  ARG   A NH2 1 
ATOM   1089 N  N   . ASP   A 1 147 ? 12.093 -23.417 37.611  1.00 39.56  ? 840  ASP   A N   1 
ATOM   1090 C  CA  . ASP   A 1 147 ? 12.748 -23.873 38.832  1.00 39.03  ? 840  ASP   A CA  1 
ATOM   1091 C  C   . ASP   A 1 147 ? 14.076 -23.191 39.097  1.00 37.66  ? 840  ASP   A C   1 
ATOM   1092 O  O   . ASP   A 1 147 ? 15.072 -23.847 39.425  1.00 37.61  ? 840  ASP   A O   1 
ATOM   1093 C  CB  . ASP   A 1 147 ? 12.888 -25.405 38.857  1.00 40.98  ? 840  ASP   A CB  1 
ATOM   1094 C  CG  . ASP   A 1 147 ? 13.162 -25.964 40.236  1.00 46.42  ? 840  ASP   A CG  1 
ATOM   1095 O  OD1 . ASP   A 1 147 ? 12.821 -25.285 41.232  1.00 47.15  ? 840  ASP   A OD1 1 
ATOM   1096 O  OD2 . ASP   A 1 147 ? 13.735 -27.066 40.322  1.00 49.53  ? 840  ASP   A OD2 1 
ATOM   1097 N  N   . LEU   A 1 148 ? 14.087 -21.864 38.967  1.00 36.53  ? 841  LEU   A N   1 
ATOM   1098 C  CA  . LEU   A 1 148 ? 15.298 -21.108 39.253  1.00 35.73  ? 841  LEU   A CA  1 
ATOM   1099 C  C   . LEU   A 1 148 ? 15.431 -20.972 40.753  1.00 35.82  ? 841  LEU   A C   1 
ATOM   1100 O  O   . LEU   A 1 148 ? 14.491 -20.557 41.419  1.00 36.64  ? 841  LEU   A O   1 
ATOM   1101 C  CB  . LEU   A 1 148 ? 15.319 -19.742 38.558  1.00 34.49  ? 841  LEU   A CB  1 
ATOM   1102 C  CG  . LEU   A 1 148 ? 16.546 -18.900 38.830  1.00 33.93  ? 841  LEU   A CG  1 
ATOM   1103 C  CD1 . LEU   A 1 148 ? 17.846 -19.607 38.385  1.00 32.92  ? 841  LEU   A CD1 1 
ATOM   1104 C  CD2 . LEU   A 1 148 ? 16.399 -17.545 38.195  1.00 34.79  ? 841  LEU   A CD2 1 
ATOM   1105 N  N   . ALA   A 1 149 ? 16.567 -21.393 41.282  1.00 34.99  ? 842  ALA   A N   1 
ATOM   1106 C  CA  . ALA   A 1 149 ? 16.877 -21.338 42.702  1.00 35.21  ? 842  ALA   A CA  1 
ATOM   1107 C  C   . ALA   A 1 149 ? 18.396 -21.351 42.836  1.00 35.79  ? 842  ALA   A C   1 
ATOM   1108 O  O   . ALA   A 1 149 ? 19.078 -21.693 41.873  1.00 36.21  ? 842  ALA   A O   1 
ATOM   1109 C  CB  . ALA   A 1 149 ? 16.268 -22.543 43.414  1.00 35.33  ? 842  ALA   A CB  1 
ATOM   1110 N  N   . ALA   A 1 150 ? 18.942 -21.002 44.008  1.00 36.19  ? 843  ALA   A N   1 
ATOM   1111 C  CA  . ALA   A 1 150 ? 20.392 -21.018 44.199  1.00 37.13  ? 843  ALA   A CA  1 
ATOM   1112 C  C   . ALA   A 1 150 ? 20.975 -22.432 44.029  1.00 38.07  ? 843  ALA   A C   1 
ATOM   1113 O  O   . ALA   A 1 150 ? 22.127 -22.573 43.617  1.00 38.27  ? 843  ALA   A O   1 
ATOM   1114 C  CB  . ALA   A 1 150 ? 20.759 -20.429 45.553  1.00 37.34  ? 843  ALA   A CB  1 
ATOM   1115 N  N   . ARG   A 1 151 ? 20.166 -23.478 44.281  1.00 38.38  ? 844  ARG   A N   1 
ATOM   1116 C  CA  . ARG   A 1 151 ? 20.572 -24.872 44.080  1.00 38.90  ? 844  ARG   A CA  1 
ATOM   1117 C  C   . ARG   A 1 151 ? 20.753 -25.211 42.585  1.00 38.58  ? 844  ARG   A C   1 
ATOM   1118 O  O   . ARG   A 1 151 ? 21.504 -26.127 42.247  1.00 38.65  ? 844  ARG   A O   1 
ATOM   1119 C  CB  . ARG   A 1 151 ? 19.559 -25.838 44.728  1.00 41.35  ? 844  ARG   A CB  1 
ATOM   1120 C  CG  . ARG   A 1 151 ? 18.182 -25.817 44.066  1.00 47.07  ? 844  ARG   A CG  1 
ATOM   1121 C  CD  . ARG   A 1 151 ? 17.145 -26.739 44.706  1.00 52.00  ? 844  ARG   A CD  1 
ATOM   1122 N  NE  . ARG   A 1 151 ? 15.812 -26.558 44.105  1.00 56.43  ? 844  ARG   A NE  1 
ATOM   1123 C  CZ  . ARG   A 1 151 ? 14.886 -25.708 44.569  1.00 58.10  ? 844  ARG   A CZ  1 
ATOM   1124 N  NH1 . ARG   A 1 151 ? 13.713 -25.591 43.953  1.00 57.54  ? 844  ARG   A NH1 1 
ATOM   1125 N  NH2 . ARG   A 1 151 ? 15.129 -24.974 45.650  1.00 56.89  ? 844  ARG   A NH2 1 
ATOM   1126 N  N   . ASN   A 1 152 ? 20.073 -24.468 41.689  1.00 38.33  ? 845  ASN   A N   1 
ATOM   1127 C  CA  . ASN   A 1 152 ? 20.152 -24.700 40.245  1.00 37.97  ? 845  ASN   A CA  1 
ATOM   1128 C  C   . ASN   A 1 152 ? 21.081 -23.722 39.502  1.00 37.93  ? 845  ASN   A C   1 
ATOM   1129 O  O   . ASN   A 1 152 ? 20.964 -23.531 38.295  1.00 38.61  ? 845  ASN   A O   1 
ATOM   1130 C  CB  . ASN   A 1 152 ? 18.756 -24.735 39.626  1.00 38.41  ? 845  ASN   A CB  1 
ATOM   1131 C  CG  . ASN   A 1 152 ? 17.939 -25.911 40.125  1.00 40.72  ? 845  ASN   A CG  1 
ATOM   1132 O  OD1 . ASN   A 1 152 ? 16.742 -25.798 40.413  1.00 41.22  ? 845  ASN   A OD1 1 
ATOM   1133 N  ND2 . ASN   A 1 152 ? 18.580 -27.073 40.258  1.00 42.14  ? 845  ASN   A ND2 1 
ATOM   1134 N  N   . VAL   A 1 153 ? 22.016 -23.135 40.216  1.00 37.47  ? 846  VAL   A N   1 
ATOM   1135 C  CA  . VAL   A 1 153 ? 23.016 -22.258 39.654  1.00 38.02  ? 846  VAL   A CA  1 
ATOM   1136 C  C   . VAL   A 1 153 ? 24.302 -22.943 40.057  1.00 38.95  ? 846  VAL   A C   1 
ATOM   1137 O  O   . VAL   A 1 153 ? 24.541 -23.148 41.247  1.00 39.24  ? 846  VAL   A O   1 
ATOM   1138 C  CB  . VAL   A 1 153 ? 22.933 -20.829 40.228  1.00 38.69  ? 846  VAL   A CB  1 
ATOM   1139 C  CG1 . VAL   A 1 153 ? 24.103 -19.987 39.727  1.00 39.21  ? 846  VAL   A CG1 1 
ATOM   1140 C  CG2 . VAL   A 1 153 ? 21.593 -20.169 39.888  1.00 38.77  ? 846  VAL   A CG2 1 
ATOM   1141 N  N   . LEU   A 1 154 ? 25.088 -23.384 39.078  1.00 38.86  ? 847  LEU   A N   1 
ATOM   1142 C  CA  . LEU   A 1 154 ? 26.314 -24.114 39.355  1.00 38.74  ? 847  LEU   A CA  1 
ATOM   1143 C  C   . LEU   A 1 154 ? 27.541 -23.238 39.252  1.00 38.89  ? 847  LEU   A C   1 
ATOM   1144 O  O   . LEU   A 1 154 ? 27.544 -22.258 38.520  1.00 38.84  ? 847  LEU   A O   1 
ATOM   1145 C  CB  . LEU   A 1 154 ? 26.437 -25.347 38.453  1.00 38.32  ? 847  LEU   A CB  1 
ATOM   1146 C  CG  . LEU   A 1 154 ? 25.213 -26.203 38.300  1.00 38.45  ? 847  LEU   A CG  1 
ATOM   1147 C  CD1 . LEU   A 1 154 ? 25.507 -27.332 37.352  1.00 38.84  ? 847  LEU   A CD1 1 
ATOM   1148 C  CD2 . LEU   A 1 154 ? 24.740 -26.721 39.628  1.00 38.60  ? 847  LEU   A CD2 1 
ATOM   1149 N  N   . VAL   A 1 155 ? 28.587 -23.603 39.981  1.00 39.24  ? 848  VAL   A N   1 
ATOM   1150 C  CA  . VAL   A 1 155 ? 29.815 -22.833 40.005  1.00 40.48  ? 848  VAL   A CA  1 
ATOM   1151 C  C   . VAL   A 1 155 ? 30.943 -23.512 39.194  1.00 41.79  ? 848  VAL   A C   1 
ATOM   1152 O  O   . VAL   A 1 155 ? 31.510 -24.517 39.639  1.00 42.08  ? 848  VAL   A O   1 
ATOM   1153 C  CB  . VAL   A 1 155 ? 30.249 -22.563 41.470  1.00 40.86  ? 848  VAL   A CB  1 
ATOM   1154 C  CG1 . VAL   A 1 155 ? 31.434 -21.625 41.520  1.00 41.00  ? 848  VAL   A CG1 1 
ATOM   1155 C  CG2 . VAL   A 1 155 ? 29.099 -22.001 42.301  1.00 41.27  ? 848  VAL   A CG2 1 
ATOM   1156 N  N   . LYS   A 1 156 ? 31.259 -22.963 38.007  1.00 42.33  ? 849  LYS   A N   1 
ATOM   1157 C  CA  . LYS   A 1 156 ? 32.349 -23.484 37.185  1.00 43.48  ? 849  LYS   A CA  1 
ATOM   1158 C  C   . LYS   A 1 156 ? 33.653 -23.060 37.873  1.00 44.39  ? 849  LYS   A C   1 
ATOM   1159 O  O   . LYS   A 1 156 ? 34.514 -23.890 38.147  1.00 44.61  ? 849  LYS   A O   1 
ATOM   1160 C  CB  . LYS   A 1 156 ? 32.254 -22.937 35.747  1.00 44.85  ? 849  LYS   A CB  1 
ATOM   1161 C  CG  . LYS   A 1 156 ? 33.328 -23.472 34.828  1.00 48.27  ? 849  LYS   A CG  1 
ATOM   1162 C  CD  . LYS   A 1 156 ? 32.919 -23.290 33.382  1.00 52.41  ? 849  LYS   A CD  1 
ATOM   1163 C  CE  . LYS   A 1 156 ? 33.913 -23.893 32.419  1.00 55.10  ? 849  LYS   A CE  1 
ATOM   1164 N  NZ  . LYS   A 1 156 ? 34.963 -22.917 32.032  1.00 57.22  ? 849  LYS   A NZ  1 
ATOM   1165 N  N   . THR   A 1 157 ? 33.767 -21.762 38.174  1.00 44.61  ? 850  THR   A N   1 
ATOM   1166 C  CA  . THR   A 1 157 ? 34.836 -21.104 38.940  1.00 45.14  ? 850  THR   A CA  1 
ATOM   1167 C  C   . THR   A 1 157 ? 34.133 -20.080 39.845  1.00 45.44  ? 850  THR   A C   1 
ATOM   1168 O  O   . THR   A 1 157 ? 33.012 -19.667 39.521  1.00 45.46  ? 850  THR   A O   1 
ATOM   1169 C  CB  . THR   A 1 157 ? 35.893 -20.411 38.023  1.00 46.32  ? 850  THR   A CB  1 
ATOM   1170 O  OG1 . THR   A 1 157 ? 35.414 -19.175 37.506  1.00 47.21  ? 850  THR   A OG1 1 
ATOM   1171 C  CG2 . THR   A 1 157 ? 36.379 -21.286 36.904  1.00 46.78  ? 850  THR   A CG2 1 
ATOM   1172 N  N   . PRO   A 1 158 ? 34.761 -19.585 40.931  1.00 45.57  ? 851  PRO   A N   1 
ATOM   1173 C  CA  . PRO   A 1 158 ? 34.088 -18.573 41.764  1.00 45.25  ? 851  PRO   A CA  1 
ATOM   1174 C  C   . PRO   A 1 158 ? 33.612 -17.343 40.980  1.00 45.20  ? 851  PRO   A C   1 
ATOM   1175 O  O   . PRO   A 1 158 ? 32.685 -16.672 41.415  1.00 45.89  ? 851  PRO   A O   1 
ATOM   1176 C  CB  . PRO   A 1 158 ? 35.144 -18.220 42.814  1.00 46.08  ? 851  PRO   A CB  1 
ATOM   1177 C  CG  . PRO   A 1 158 ? 35.997 -19.427 42.910  1.00 46.87  ? 851  PRO   A CG  1 
ATOM   1178 C  CD  . PRO   A 1 158 ? 36.081 -19.938 41.486  1.00 45.44  ? 851  PRO   A CD  1 
ATOM   1179 N  N   . GLN   A 1 159 ? 34.201 -17.069 39.806  1.00 44.32  ? 852  GLN   A N   1 
ATOM   1180 C  CA  . GLN   A 1 159 ? 33.777 -15.948 38.977  1.00 43.74  ? 852  GLN   A CA  1 
ATOM   1181 C  C   . GLN   A 1 159 ? 33.020 -16.366 37.709  1.00 41.59  ? 852  GLN   A C   1 
ATOM   1182 O  O   . GLN   A 1 159 ? 32.856 -15.549 36.816  1.00 41.40  ? 852  GLN   A O   1 
ATOM   1183 C  CB  . GLN   A 1 159 ? 34.950 -15.018 38.637  1.00 47.01  ? 852  GLN   A CB  1 
ATOM   1184 C  CG  . GLN   A 1 159 ? 36.216 -15.726 38.162  1.00 53.73  ? 852  GLN   A CG  1 
ATOM   1185 C  CD  . GLN   A 1 159 ? 37.155 -16.104 39.292  1.00 61.53  ? 852  GLN   A CD  1 
ATOM   1186 O  OE1 . GLN   A 1 159 ? 37.791 -17.175 39.275  1.00 64.16  ? 852  GLN   A OE1 1 
ATOM   1187 N  NE2 . GLN   A 1 159 ? 37.261 -15.241 40.300  1.00 62.09  ? 852  GLN   A NE2 1 
ATOM   1188 N  N   . HIS   A 1 160 ? 32.524 -17.609 37.636  1.00 39.93  ? 853  HIS   A N   1 
ATOM   1189 C  CA  . HIS   A 1 160 ? 31.776 -18.080 36.472  1.00 38.95  ? 853  HIS   A CA  1 
ATOM   1190 C  C   . HIS   A 1 160 ? 30.675 -19.041 36.893  1.00 37.38  ? 853  HIS   A C   1 
ATOM   1191 O  O   . HIS   A 1 160 ? 30.936 -20.209 37.171  1.00 37.18  ? 853  HIS   A O   1 
ATOM   1192 C  CB  . HIS   A 1 160 ? 32.719 -18.730 35.447  1.00 40.00  ? 853  HIS   A CB  1 
ATOM   1193 C  CG  . HIS   A 1 160 ? 32.072 -19.076 34.135  1.00 42.93  ? 853  HIS   A CG  1 
ATOM   1194 N  ND1 . HIS   A 1 160 ? 32.835 -19.360 33.011  1.00 44.93  ? 853  HIS   A ND1 1 
ATOM   1195 C  CD2 . HIS   A 1 160 ? 30.761 -19.180 33.803  1.00 44.28  ? 853  HIS   A CD2 1 
ATOM   1196 C  CE1 . HIS   A 1 160 ? 31.967 -19.633 32.048  1.00 45.55  ? 853  HIS   A CE1 1 
ATOM   1197 N  NE2 . HIS   A 1 160 ? 30.710 -19.532 32.476  1.00 45.39  ? 853  HIS   A NE2 1 
ATOM   1198 N  N   . VAL   A 1 161 ? 29.438 -18.539 36.928  1.00 36.43  ? 854  VAL   A N   1 
ATOM   1199 C  CA  . VAL   A 1 161 ? 28.271 -19.328 37.315  1.00 35.95  ? 854  VAL   A CA  1 
ATOM   1200 C  C   . VAL   A 1 161 ? 27.395 -19.617 36.101  1.00 35.66  ? 854  VAL   A C   1 
ATOM   1201 O  O   . VAL   A 1 161 ? 27.390 -18.843 35.140  1.00 35.85  ? 854  VAL   A O   1 
ATOM   1202 C  CB  . VAL   A 1 161 ? 27.462 -18.744 38.524  1.00 35.95  ? 854  VAL   A CB  1 
ATOM   1203 C  CG1 . VAL   A 1 161 ? 28.372 -18.411 39.700  1.00 36.11  ? 854  VAL   A CG1 1 
ATOM   1204 C  CG2 . VAL   A 1 161 ? 26.632 -17.532 38.121  1.00 35.85  ? 854  VAL   A CG2 1 
ATOM   1205 N  N   . LYS   A 1 162 ? 26.680 -20.761 36.132  1.00 35.02  ? 855  LYS   A N   1 
ATOM   1206 C  CA  . LYS   A 1 162 ? 25.815 -21.220 35.046  1.00 34.43  ? 855  LYS   A CA  1 
ATOM   1207 C  C   . LYS   A 1 162 ? 24.486 -21.755 35.568  1.00 34.49  ? 855  LYS   A C   1 
ATOM   1208 O  O   . LYS   A 1 162 ? 24.446 -22.341 36.628  1.00 34.57  ? 855  LYS   A O   1 
ATOM   1209 C  CB  . LYS   A 1 162 ? 26.517 -22.332 34.271  1.00 35.17  ? 855  LYS   A CB  1 
ATOM   1210 C  CG  . LYS   A 1 162 ? 27.710 -21.880 33.467  1.00 37.44  ? 855  LYS   A CG  1 
ATOM   1211 C  CD  . LYS   A 1 162 ? 28.661 -23.008 33.262  1.00 40.76  ? 855  LYS   A CD  1 
ATOM   1212 C  CE  . LYS   A 1 162 ? 29.387 -22.864 31.969  1.00 43.84  ? 855  LYS   A CE  1 
ATOM   1213 N  NZ  . LYS   A 1 162 ? 28.496 -23.150 30.817  1.00 46.28  ? 855  LYS   A NZ  1 
ATOM   1214 N  N   . ILE   A 1 163 ? 23.413 -21.604 34.805  1.00 34.83  ? 856  ILE   A N   1 
ATOM   1215 C  CA  . ILE   A 1 163 ? 22.091 -22.095 35.183  1.00 36.06  ? 856  ILE   A CA  1 
ATOM   1216 C  C   . ILE   A 1 163 ? 21.855 -23.496 34.633  1.00 37.43  ? 856  ILE   A C   1 
ATOM   1217 O  O   . ILE   A 1 163 ? 21.951 -23.723 33.421  1.00 37.64  ? 856  ILE   A O   1 
ATOM   1218 C  CB  . ILE   A 1 163 ? 20.987 -21.114 34.708  1.00 36.57  ? 856  ILE   A CB  1 
ATOM   1219 C  CG1 . ILE   A 1 163 ? 21.187 -19.718 35.332  1.00 37.43  ? 856  ILE   A CG1 1 
ATOM   1220 C  CG2 . ILE   A 1 163 ? 19.584 -21.662 34.984  1.00 36.73  ? 856  ILE   A CG2 1 
ATOM   1221 C  CD1 . ILE   A 1 163 ? 20.508 -18.684 34.652  1.00 38.27  ? 856  ILE   A CD1 1 
ATOM   1222 N  N   . THR   A 1 164 ? 21.520 -24.435 35.523  1.00 37.86  ? 857  THR   A N   1 
ATOM   1223 C  CA  . THR   A 1 164 ? 21.236 -25.809 35.131  1.00 38.94  ? 857  THR   A CA  1 
ATOM   1224 C  C   . THR   A 1 164 ? 19.725 -26.128 35.292  1.00 40.35  ? 857  THR   A C   1 
ATOM   1225 O  O   . THR   A 1 164 ? 18.967 -25.302 35.811  1.00 40.65  ? 857  THR   A O   1 
ATOM   1226 C  CB  . THR   A 1 164 ? 22.115 -26.764 35.969  1.00 39.69  ? 857  THR   A CB  1 
ATOM   1227 O  OG1 . THR   A 1 164 ? 21.972 -28.074 35.440  1.00 40.79  ? 857  THR   A OG1 1 
ATOM   1228 C  CG2 . THR   A 1 164 ? 21.725 -26.791 37.451  1.00 39.17  ? 857  THR   A CG2 1 
ATOM   1229 N  N   . ASP   A 1 165 ? 19.301 -27.308 34.815  1.00 40.84  ? 858  ASP   A N   1 
ATOM   1230 C  CA  . ASP   A 1 165 ? 17.971 -27.876 34.957  1.00 42.22  ? 858  ASP   A CA  1 
ATOM   1231 C  C   . ASP   A 1 165 ? 16.862 -27.125 34.227  1.00 43.23  ? 858  ASP   A C   1 
ATOM   1232 O  O   . ASP   A 1 165 ? 15.705 -27.167 34.655  1.00 43.73  ? 858  ASP   A O   1 
ATOM   1233 C  CB  . ASP   A 1 165 ? 17.605 -28.091 36.437  1.00 43.99  ? 858  ASP   A CB  1 
ATOM   1234 C  CG  . ASP   A 1 165 ? 18.548 -29.029 37.185  1.00 49.14  ? 858  ASP   A CG  1 
ATOM   1235 O  OD1 . ASP   A 1 165 ? 19.562 -29.466 36.584  1.00 49.56  ? 858  ASP   A OD1 1 
ATOM   1236 O  OD2 . ASP   A 1 165 ? 18.276 -29.324 38.381  1.00 51.80  ? 858  ASP   A OD2 1 
ATOM   1237 N  N   . PHE   A 1 166 ? 17.189 -26.504 33.100  1.00 43.21  ? 859  PHE   A N   1 
ATOM   1238 C  CA  . PHE   A 1 166 ? 16.164 -25.891 32.246  1.00 43.61  ? 859  PHE   A CA  1 
ATOM   1239 C  C   . PHE   A 1 166 ? 15.477 -27.049 31.488  1.00 44.98  ? 859  PHE   A C   1 
ATOM   1240 O  O   . PHE   A 1 166 ? 16.100 -28.077 31.200  1.00 45.05  ? 859  PHE   A O   1 
ATOM   1241 C  CB  . PHE   A 1 166 ? 16.749 -24.843 31.268  1.00 42.61  ? 859  PHE   A CB  1 
ATOM   1242 C  CG  . PHE   A 1 166 ? 18.051 -25.261 30.633  1.00 42.46  ? 859  PHE   A CG  1 
ATOM   1243 C  CD1 . PHE   A 1 166 ? 18.064 -26.026 29.477  1.00 42.88  ? 859  PHE   A CD1 1 
ATOM   1244 C  CD2 . PHE   A 1 166 ? 19.263 -24.941 31.221  1.00 42.81  ? 859  PHE   A CD2 1 
ATOM   1245 C  CE1 . PHE   A 1 166 ? 19.259 -26.478 28.937  1.00 43.06  ? 859  PHE   A CE1 1 
ATOM   1246 C  CE2 . PHE   A 1 166 ? 20.455 -25.394 30.672  1.00 43.26  ? 859  PHE   A CE2 1 
ATOM   1247 C  CZ  . PHE   A 1 166 ? 20.446 -26.115 29.506  1.00 42.65  ? 859  PHE   A CZ  1 
ATOM   1248 N  N   . GLY   A 1 167 ? 14.182 -26.915 31.257  1.00 45.83  ? 860  GLY   A N   1 
ATOM   1249 C  CA  . GLY   A 1 167 ? 13.413 -27.943 30.567  1.00 46.78  ? 860  GLY   A CA  1 
ATOM   1250 C  C   . GLY   A 1 167 ? 13.254 -29.249 31.315  1.00 47.70  ? 860  GLY   A C   1 
ATOM   1251 O  O   . GLY   A 1 167 ? 12.713 -30.203 30.763  1.00 48.08  ? 860  GLY   A O   1 
ATOM   1252 N  N   . LEU   A 1 168 ? 13.729 -29.315 32.564  1.00 48.21  ? 861  LEU   A N   1 
ATOM   1253 C  CA  . LEU   A 1 168 ? 13.632 -30.520 33.375  1.00 49.27  ? 861  LEU   A CA  1 
ATOM   1254 C  C   . LEU   A 1 168 ? 12.211 -30.696 33.879  1.00 51.07  ? 861  LEU   A C   1 
ATOM   1255 O  O   . LEU   A 1 168 ? 11.720 -31.813 33.883  1.00 51.81  ? 861  LEU   A O   1 
ATOM   1256 C  CB  . LEU   A 1 168 ? 14.630 -30.481 34.546  1.00 49.12  ? 861  LEU   A CB  1 
ATOM   1257 C  CG  . LEU   A 1 168 ? 14.625 -31.679 35.489  1.00 49.96  ? 861  LEU   A CG  1 
ATOM   1258 C  CD1 . LEU   A 1 168 ? 14.965 -32.947 34.752  1.00 50.65  ? 861  LEU   A CD1 1 
ATOM   1259 C  CD2 . LEU   A 1 168 ? 15.608 -31.488 36.601  1.00 50.27  ? 861  LEU   A CD2 1 
ATOM   1260 N  N   . ALA   A 1 169 ? 11.527 -29.606 34.259  1.00 51.78  ? 862  ALA   A N   1 
ATOM   1261 C  CA  . ALA   A 1 169 ? 10.142 -29.699 34.720  1.00 52.90  ? 862  ALA   A CA  1 
ATOM   1262 C  C   . ALA   A 1 169 ? 9.223  -30.246 33.632  1.00 53.90  ? 862  ALA   A C   1 
ATOM   1263 O  O   . ALA   A 1 169 ? 8.383  -31.080 33.930  1.00 53.75  ? 862  ALA   A O   1 
ATOM   1264 C  CB  . ALA   A 1 169 ? 9.648  -28.347 35.203  1.00 53.29  ? 862  ALA   A CB  1 
ATOM   1265 N  N   . LYS   A 1 170 ? 9.420  -29.838 32.367  1.00 54.84  ? 863  LYS   A N   1 
ATOM   1266 C  CA  . LYS   A 1 170 ? 8.611  -30.353 31.264  1.00 56.31  ? 863  LYS   A CA  1 
ATOM   1267 C  C   . LYS   A 1 170 ? 8.889  -31.834 31.081  1.00 58.03  ? 863  LYS   A C   1 
ATOM   1268 O  O   . LYS   A 1 170 ? 7.946  -32.622 31.011  1.00 58.65  ? 863  LYS   A O   1 
ATOM   1269 C  CB  . LYS   A 1 170 ? 8.877  -29.585 29.962  1.00 58.24  ? 863  LYS   A CB  1 
ATOM   1270 C  CG  . LYS   A 1 170 ? 7.954  -30.007 28.829  1.00 63.06  ? 863  LYS   A CG  1 
ATOM   1271 C  CD  . LYS   A 1 170 ? 8.125  -29.124 27.598  1.00 68.42  ? 863  LYS   A CD  1 
ATOM   1272 C  CE  . LYS   A 1 170 ? 7.129  -29.413 26.492  1.00 72.11  ? 863  LYS   A CE  1 
ATOM   1273 N  NZ  . LYS   A 1 170 ? 7.437  -28.640 25.250  1.00 74.00  ? 863  LYS   A NZ  1 
ATOM   1274 N  N   . LEU   A 1 171 ? 10.185 -32.218 31.105  1.00 58.62  ? 864  LEU   A N   1 
ATOM   1275 C  CA  . LEU   A 1 171 ? 10.691 -33.593 30.983  1.00 59.31  ? 864  LEU   A CA  1 
ATOM   1276 C  C   . LEU   A 1 171 ? 10.031 -34.491 32.038  1.00 60.04  ? 864  LEU   A C   1 
ATOM   1277 O  O   . LEU   A 1 171 ? 9.589  -35.588 31.714  1.00 60.28  ? 864  LEU   A O   1 
ATOM   1278 C  CB  . LEU   A 1 171 ? 12.230 -33.577 31.167  1.00 59.33  ? 864  LEU   A CB  1 
ATOM   1279 C  CG  . LEU   A 1 171 ? 13.075 -34.805 30.771  1.00 60.68  ? 864  LEU   A CG  1 
ATOM   1280 C  CD1 . LEU   A 1 171 ? 13.093 -35.867 31.846  1.00 61.21  ? 864  LEU   A CD1 1 
ATOM   1281 C  CD2 . LEU   A 1 171 ? 12.718 -35.336 29.419  1.00 61.29  ? 864  LEU   A CD2 1 
ATOM   1282 N  N   . LEU   A 1 172 ? 9.938  -34.015 33.288  1.00 60.18  ? 865  LEU   A N   1 
ATOM   1283 C  CA  . LEU   A 1 172 ? 9.334  -34.786 34.365  1.00 60.97  ? 865  LEU   A CA  1 
ATOM   1284 C  C   . LEU   A 1 172 ? 7.802  -34.702 34.432  1.00 63.12  ? 865  LEU   A C   1 
ATOM   1285 O  O   . LEU   A 1 172 ? 7.212  -35.117 35.422  1.00 62.64  ? 865  LEU   A O   1 
ATOM   1286 C  CB  . LEU   A 1 172 ? 9.952  -34.404 35.711  1.00 60.55  ? 865  LEU   A CB  1 
ATOM   1287 C  CG  . LEU   A 1 172 ? 11.478 -34.403 35.801  1.00 61.17  ? 865  LEU   A CG  1 
ATOM   1288 C  CD1 . LEU   A 1 172 ? 11.933 -33.974 37.171  1.00 61.58  ? 865  LEU   A CD1 1 
ATOM   1289 C  CD2 . LEU   A 1 172 ? 12.064 -35.754 35.467  1.00 61.53  ? 865  LEU   A CD2 1 
ATOM   1290 N  N   . GLY   A 1 173 ? 7.177  -34.190 33.378  1.00 65.74  ? 866  GLY   A N   1 
ATOM   1291 C  CA  . GLY   A 1 173 ? 5.729  -34.085 33.260  1.00 69.00  ? 866  GLY   A CA  1 
ATOM   1292 C  C   . GLY   A 1 173 ? 5.030  -33.046 34.111  1.00 72.38  ? 866  GLY   A C   1 
ATOM   1293 O  O   . GLY   A 1 173 ? 3.899  -33.270 34.556  1.00 72.48  ? 866  GLY   A O   1 
ATOM   1294 N  N   . ALA   A 1 174 ? 5.673  -31.894 34.324  1.00 74.89  ? 867  ALA   A N   1 
ATOM   1295 C  CA  . ALA   A 1 174 ? 5.054  -30.810 35.084  1.00 77.87  ? 867  ALA   A CA  1 
ATOM   1296 C  C   . ALA   A 1 174 ? 4.284  -29.809 34.199  1.00 80.91  ? 867  ALA   A C   1 
ATOM   1297 O  O   . ALA   A 1 174 ? 3.746  -28.837 34.724  1.00 81.38  ? 867  ALA   A O   1 
ATOM   1298 C  CB  . ALA   A 1 174 ? 6.082  -30.088 35.937  1.00 78.17  ? 867  ALA   A CB  1 
ATOM   1299 N  N   . GLU   A 1 175 ? 4.209  -30.042 32.877  1.00 82.92  ? 868  GLU   A N   1 
ATOM   1300 C  CA  . GLU   A 1 175 ? 3.441  -29.178 31.979  1.00 85.56  ? 868  GLU   A CA  1 
ATOM   1301 C  C   . GLU   A 1 175 ? 2.204  -29.912 31.422  1.00 88.26  ? 868  GLU   A C   1 
ATOM   1302 O  O   . GLU   A 1 175 ? 1.735  -29.571 30.334  1.00 88.44  ? 868  GLU   A O   1 
ATOM   1303 C  CB  . GLU   A 1 175 ? 4.317  -28.694 30.815  1.00 87.79  ? 868  GLU   A CB  1 
ATOM   1304 C  CG  . GLU   A 1 175 ? 5.439  -27.761 31.234  1.00 92.45  ? 868  GLU   A CG  1 
ATOM   1305 C  CD  . GLU   A 1 175 ? 6.125  -27.023 30.098  1.00 98.66  ? 868  GLU   A CD  1 
ATOM   1306 O  OE1 . GLU   A 1 175 ? 7.143  -26.345 30.367  1.00 100.20 ? 868  GLU   A OE1 1 
ATOM   1307 O  OE2 . GLU   A 1 175 ? 5.643  -27.111 28.944  1.00 100.34 ? 868  GLU   A OE2 1 
ATOM   1308 N  N   . GLU   A 1 176 ? 1.685  -30.921 32.158  1.00 90.10  ? 869  GLU   A N   1 
ATOM   1309 C  CA  . GLU   A 1 176 ? 0.553  -31.744 31.737  1.00 92.15  ? 869  GLU   A CA  1 
ATOM   1310 C  C   . GLU   A 1 176 ? -0.696 -31.477 32.560  1.00 94.26  ? 869  GLU   A C   1 
ATOM   1311 O  O   . GLU   A 1 176 ? -0.609 -31.093 33.730  1.00 94.39  ? 869  GLU   A O   1 
ATOM   1312 C  CB  . GLU   A 1 176 ? 0.913  -33.232 31.858  1.00 94.16  ? 869  GLU   A CB  1 
ATOM   1313 C  CG  . GLU   A 1 176 ? 2.162  -33.621 31.094  1.00 99.53  ? 869  GLU   A CG  1 
ATOM   1314 C  CD  . GLU   A 1 176 ? 1.961  -33.727 29.596  1.00 106.56 ? 869  GLU   A CD  1 
ATOM   1315 O  OE1 . GLU   A 1 176 ? 0.861  -34.152 29.174  1.00 108.13 ? 869  GLU   A OE1 1 
ATOM   1316 O  OE2 . GLU   A 1 176 ? 2.905  -33.392 28.843  1.00 108.74 ? 869  GLU   A OE2 1 
ATOM   1317 N  N   . LYS   A 1 177 ? -1.867 -31.709 31.946  1.00 95.55  ? 870  LYS   A N   1 
ATOM   1318 C  CA  . LYS   A 1 177 ? -3.159 -31.572 32.622  1.00 97.04  ? 870  LYS   A CA  1 
ATOM   1319 C  C   . LYS   A 1 177 ? -3.567 -32.885 33.314  1.00 98.61  ? 870  LYS   A C   1 
ATOM   1320 O  O   . LYS   A 1 177 ? -4.377 -32.848 34.239  1.00 98.93  ? 870  LYS   A O   1 
ATOM   1321 C  CB  . LYS   A 1 177 ? -4.263 -31.125 31.645  1.00 98.62  ? 870  LYS   A CB  1 
ATOM   1322 C  CG  . LYS   A 1 177 ? -4.198 -29.653 31.262  1.00 102.01 ? 870  LYS   A CG  1 
ATOM   1323 C  CD  . LYS   A 1 177 ? -5.484 -29.186 30.586  1.00 105.69 ? 870  LYS   A CD  1 
ATOM   1324 C  CE  . LYS   A 1 177 ? -6.681 -29.219 31.510  1.00 108.74 ? 870  LYS   A CE  1 
ATOM   1325 N  NZ  . LYS   A 1 177 ? -6.513 -28.314 32.678  1.00 110.41 ? 870  LYS   A NZ  1 
ATOM   1326 N  N   . GLU   A 1 178 ? -3.025 -34.043 32.859  1.00 99.42  ? 871  GLU   A N   1 
ATOM   1327 C  CA  . GLU   A 1 178 ? -3.312 -35.364 33.429  1.00 100.64 ? 871  GLU   A CA  1 
ATOM   1328 C  C   . GLU   A 1 178 ? -2.270 -35.774 34.492  1.00 101.44 ? 871  GLU   A C   1 
ATOM   1329 O  O   . GLU   A 1 178 ? -2.603 -36.476 35.451  1.00 101.53 ? 871  GLU   A O   1 
ATOM   1330 C  CB  . GLU   A 1 178 ? -3.420 -36.432 32.321  1.00 102.88 ? 871  GLU   A CB  1 
ATOM   1331 C  CG  . GLU   A 1 178 ? -4.846 -36.712 31.867  1.00 107.59 ? 871  GLU   A CG  1 
ATOM   1332 C  CD  . GLU   A 1 178 ? -5.473 -35.678 30.949  1.00 113.40 ? 871  GLU   A CD  1 
ATOM   1333 O  OE1 . GLU   A 1 178 ? -4.718 -34.928 30.289  1.00 114.58 ? 871  GLU   A OE1 1 
ATOM   1334 O  OE2 . GLU   A 1 178 ? -6.722 -35.629 30.876  1.00 115.04 ? 871  GLU   A OE2 1 
ATOM   1335 N  N   . TYR   A 1 179 ? -1.016 -35.320 34.332  1.00 101.73 ? 872  TYR   A N   1 
ATOM   1336 C  CA  . TYR   A 1 179 ? 0.040  -35.638 35.291  1.00 102.34 ? 872  TYR   A CA  1 
ATOM   1337 C  C   . TYR   A 1 179 ? 0.472  -34.399 36.115  1.00 102.47 ? 872  TYR   A C   1 
ATOM   1338 O  O   . TYR   A 1 179 ? 1.079  -33.456 35.598  1.00 102.47 ? 872  TYR   A O   1 
ATOM   1339 C  CB  . TYR   A 1 179 ? 1.230  -36.350 34.605  1.00 102.57 ? 872  TYR   A CB  1 
ATOM   1340 C  CG  . TYR   A 1 179 ? 2.123  -37.113 35.563  1.00 103.54 ? 872  TYR   A CG  1 
ATOM   1341 C  CD1 . TYR   A 1 179 ? 1.818  -38.412 35.947  1.00 104.47 ? 872  TYR   A CD1 1 
ATOM   1342 C  CD2 . TYR   A 1 179 ? 3.263  -36.528 36.097  1.00 104.51 ? 872  TYR   A CD2 1 
ATOM   1343 C  CE1 . TYR   A 1 179 ? 2.624  -39.107 36.844  1.00 105.42 ? 872  TYR   A CE1 1 
ATOM   1344 C  CE2 . TYR   A 1 179 ? 4.073  -37.209 36.998  1.00 105.37 ? 872  TYR   A CE2 1 
ATOM   1345 C  CZ  . TYR   A 1 179 ? 3.754  -38.501 37.366  1.00 106.34 ? 872  TYR   A CZ  1 
ATOM   1346 O  OH  . TYR   A 1 179 ? 4.566  -39.167 38.253  1.00 107.85 ? 872  TYR   A OH  1 
ATOM   1347 N  N   . HIS   A 1 180 ? 0.099  -34.421 37.405  1.00 102.31 ? 873  HIS   A N   1 
ATOM   1348 C  CA  . HIS   A 1 180 ? 0.356  -33.442 38.473  1.00 102.39 ? 873  HIS   A CA  1 
ATOM   1349 C  C   . HIS   A 1 180 ? 0.471  -34.201 39.817  1.00 101.75 ? 873  HIS   A C   1 
ATOM   1350 O  O   . HIS   A 1 180 ? -0.084 -33.781 40.839  1.00 101.81 ? 873  HIS   A O   1 
ATOM   1351 C  CB  . HIS   A 1 180 ? -0.725 -32.333 38.546  1.00 103.49 ? 873  HIS   A CB  1 
ATOM   1352 C  CG  . HIS   A 1 180 ? -2.083 -32.735 38.064  1.00 106.30 ? 873  HIS   A CG  1 
ATOM   1353 N  ND1 . HIS   A 1 180 ? -2.793 -33.757 38.672  1.00 108.28 ? 873  HIS   A ND1 1 
ATOM   1354 C  CD2 . HIS   A 1 180 ? -2.818 -32.236 37.042  1.00 107.57 ? 873  HIS   A CD2 1 
ATOM   1355 C  CE1 . HIS   A 1 180 ? -3.932 -33.848 38.002  1.00 108.88 ? 873  HIS   A CE1 1 
ATOM   1356 N  NE2 . HIS   A 1 180 ? -3.993 -32.952 37.014  1.00 108.76 ? 873  HIS   A NE2 1 
ATOM   1357 N  N   . ALA   A 1 181 ? 1.218  -35.326 39.801  1.00 100.76 ? 874  ALA   A N   1 
ATOM   1358 C  CA  . ALA   A 1 181 ? 1.457  -36.179 40.967  1.00 100.01 ? 874  ALA   A CA  1 
ATOM   1359 C  C   . ALA   A 1 181 ? 2.695  -35.696 41.741  1.00 98.73  ? 874  ALA   A C   1 
ATOM   1360 O  O   . ALA   A 1 181 ? 3.571  -36.490 42.100  1.00 98.75  ? 874  ALA   A O   1 
ATOM   1361 C  CB  . ALA   A 1 181 ? 1.635  -37.628 40.525  1.00 100.19 ? 874  ALA   A CB  1 
ATOM   1362 N  N   . GLU   A 1 182 ? 2.758  -34.377 41.988  1.00 97.45  ? 875  GLU   A N   1 
ATOM   1363 C  CA  . GLU   A 1 182 ? 3.860  -33.727 42.699  1.00 96.40  ? 875  GLU   A CA  1 
ATOM   1364 C  C   . GLU   A 1 182 ? 3.339  -33.153 44.021  1.00 94.77  ? 875  GLU   A C   1 
ATOM   1365 O  O   . GLU   A 1 182 ? 2.826  -32.034 44.045  1.00 94.98  ? 875  GLU   A O   1 
ATOM   1366 C  CB  . GLU   A 1 182 ? 4.474  -32.608 41.830  1.00 98.33  ? 875  GLU   A CB  1 
ATOM   1367 C  CG  . GLU   A 1 182 ? 4.789  -33.038 40.398  1.00 102.06 ? 875  GLU   A CG  1 
ATOM   1368 C  CD  . GLU   A 1 182 ? 3.984  -32.355 39.306  1.00 106.16 ? 875  GLU   A CD  1 
ATOM   1369 O  OE1 . GLU   A 1 182 ? 3.067  -31.575 39.649  1.00 106.51 ? 875  GLU   A OE1 1 
ATOM   1370 O  OE2 . GLU   A 1 182 ? 4.271  -32.599 38.110  1.00 107.68 ? 875  GLU   A OE2 1 
ATOM   1371 N  N   . GLY   A 1 183 ? 3.447  -33.941 45.094  1.00 92.94  ? 876  GLY   A N   1 
ATOM   1372 C  CA  . GLY   A 1 183 ? 2.976  -33.564 46.424  1.00 91.51  ? 876  GLY   A CA  1 
ATOM   1373 C  C   . GLY   A 1 183 ? 3.821  -32.503 47.100  1.00 89.40  ? 876  GLY   A C   1 
ATOM   1374 O  O   . GLY   A 1 183 ? 3.576  -31.306 46.927  1.00 89.51  ? 876  GLY   A O   1 
ATOM   1375 N  N   . GLY   A 1 184 ? 4.808  -32.944 47.874  1.00 87.08  ? 877  GLY   A N   1 
ATOM   1376 C  CA  . GLY   A 1 184 ? 5.710  -32.037 48.574  1.00 85.07  ? 877  GLY   A CA  1 
ATOM   1377 C  C   . GLY   A 1 184 ? 6.973  -31.683 47.808  1.00 82.44  ? 877  GLY   A C   1 
ATOM   1378 O  O   . GLY   A 1 184 ? 7.881  -31.068 48.373  1.00 82.63  ? 877  GLY   A O   1 
ATOM   1379 N  N   . LYS   A 1 185 ? 7.061  -32.065 46.525  1.00 79.76  ? 878  LYS   A N   1 
ATOM   1380 C  CA  . LYS   A 1 185 ? 8.244  -31.769 45.720  1.00 77.53  ? 878  LYS   A CA  1 
ATOM   1381 C  C   . LYS   A 1 185 ? 8.224  -30.357 45.115  1.00 74.68  ? 878  LYS   A C   1 
ATOM   1382 O  O   . LYS   A 1 185 ? 9.289  -29.842 44.766  1.00 74.93  ? 878  LYS   A O   1 
ATOM   1383 C  CB  . LYS   A 1 185 ? 8.395  -32.805 44.591  1.00 79.30  ? 878  LYS   A CB  1 
ATOM   1384 C  CG  . LYS   A 1 185 ? 8.634  -34.230 45.067  1.00 82.92  ? 878  LYS   A CG  1 
ATOM   1385 C  CD  . LYS   A 1 185 ? 8.296  -35.245 43.978  1.00 86.54  ? 878  LYS   A CD  1 
ATOM   1386 C  CE  . LYS   A 1 185 ? 6.823  -35.253 43.634  1.00 89.70  ? 878  LYS   A CE  1 
ATOM   1387 N  NZ  . LYS   A 1 185 ? 5.979  -35.521 44.829  1.00 91.89  ? 878  LYS   A NZ  1 
ATOM   1388 N  N   . VAL   A 1 186 ? 7.023  -29.742 44.980  1.00 71.69  ? 879  VAL   A N   1 
ATOM   1389 C  CA  . VAL   A 1 186 ? 6.800  -28.441 44.324  1.00 69.08  ? 879  VAL   A CA  1 
ATOM   1390 C  C   . VAL   A 1 186 ? 7.461  -27.266 45.111  1.00 66.02  ? 879  VAL   A C   1 
ATOM   1391 O  O   . VAL   A 1 186 ? 7.349  -27.190 46.337  1.00 66.16  ? 879  VAL   A O   1 
ATOM   1392 C  CB  . VAL   A 1 186 ? 5.283  -28.228 44.004  1.00 69.24  ? 879  VAL   A CB  1 
ATOM   1393 C  CG1 . VAL   A 1 186 ? 4.412  -28.549 45.196  1.00 70.11  ? 879  VAL   A CG1 1 
ATOM   1394 C  CG2 . VAL   A 1 186 ? 4.976  -26.838 43.476  1.00 69.04  ? 879  VAL   A CG2 1 
ATOM   1395 N  N   . PRO   A 1 187 ? 8.239  -26.400 44.405  1.00 62.94  ? 880  PRO   A N   1 
ATOM   1396 C  CA  . PRO   A 1 187 ? 8.959  -25.312 45.097  1.00 60.56  ? 880  PRO   A CA  1 
ATOM   1397 C  C   . PRO   A 1 187 ? 8.143  -24.044 45.384  1.00 56.94  ? 880  PRO   A C   1 
ATOM   1398 O  O   . PRO   A 1 187 ? 8.424  -22.986 44.830  1.00 57.11  ? 880  PRO   A O   1 
ATOM   1399 C  CB  . PRO   A 1 187 ? 10.139 -25.028 44.157  1.00 61.83  ? 880  PRO   A CB  1 
ATOM   1400 C  CG  . PRO   A 1 187 ? 9.643  -25.396 42.803  1.00 62.79  ? 880  PRO   A CG  1 
ATOM   1401 C  CD  . PRO   A 1 187 ? 8.528  -26.405 42.954  1.00 61.76  ? 880  PRO   A CD  1 
ATOM   1402 N  N   . ILE   A 1 188 ? 7.173  -24.154 46.288  1.00 53.58  ? 881  ILE   A N   1 
ATOM   1403 C  CA  . ILE   A 1 188 ? 6.253  -23.087 46.680  1.00 51.11  ? 881  ILE   A CA  1 
ATOM   1404 C  C   . ILE   A 1 188 ? 6.945  -21.786 47.195  1.00 48.71  ? 881  ILE   A C   1 
ATOM   1405 O  O   . ILE   A 1 188 ? 6.484  -20.678 46.913  1.00 48.58  ? 881  ILE   A O   1 
ATOM   1406 C  CB  . ILE   A 1 188 ? 5.275  -23.703 47.720  1.00 51.01  ? 881  ILE   A CB  1 
ATOM   1407 C  CG1 . ILE   A 1 188 ? 4.383  -24.753 47.055  1.00 51.18  ? 881  ILE   A CG1 1 
ATOM   1408 C  CG2 . ILE   A 1 188 ? 4.446  -22.650 48.443  1.00 51.66  ? 881  ILE   A CG2 1 
ATOM   1409 C  CD1 . ILE   A 1 188 ? 3.498  -24.221 45.924  1.00 51.88  ? 881  ILE   A CD1 1 
ATOM   1410 N  N   . LYS   A 1 189 ? 8.069  -21.925 47.904  1.00 46.83  ? 882  LYS   A N   1 
ATOM   1411 C  CA  . LYS   A 1 189 ? 8.795  -20.787 48.466  1.00 45.32  ? 882  LYS   A CA  1 
ATOM   1412 C  C   . LYS   A 1 189 ? 9.672  -20.020 47.459  1.00 43.91  ? 882  LYS   A C   1 
ATOM   1413 O  O   . LYS   A 1 189 ? 10.298 -19.024 47.829  1.00 44.08  ? 882  LYS   A O   1 
ATOM   1414 C  CB  . LYS   A 1 189 ? 9.602  -21.226 49.686  1.00 46.84  ? 882  LYS   A CB  1 
ATOM   1415 C  CG  . LYS   A 1 189 ? 8.676  -21.761 50.771  1.00 50.82  ? 882  LYS   A CG  1 
ATOM   1416 C  CD  . LYS   A 1 189 ? 9.391  -22.217 52.013  1.00 55.15  ? 882  LYS   A CD  1 
ATOM   1417 C  CE  . LYS   A 1 189 ? 8.404  -22.666 53.065  1.00 58.45  ? 882  LYS   A CE  1 
ATOM   1418 N  NZ  . LYS   A 1 189 ? 9.081  -22.926 54.362  1.00 61.30  ? 882  LYS   A NZ  1 
ATOM   1419 N  N   . TRP   A 1 190 ? 9.685  -20.460 46.186  1.00 42.18  ? 883  TRP   A N   1 
ATOM   1420 C  CA  . TRP   A 1 190 ? 10.363 -19.806 45.060  1.00 40.51  ? 883  TRP   A CA  1 
ATOM   1421 C  C   . TRP   A 1 190 ? 9.356  -19.424 43.956  1.00 40.19  ? 883  TRP   A C   1 
ATOM   1422 O  O   . TRP   A 1 190 ? 9.745  -18.788 42.981  1.00 39.77  ? 883  TRP   A O   1 
ATOM   1423 C  CB  . TRP   A 1 190 ? 11.426 -20.735 44.452  1.00 39.53  ? 883  TRP   A CB  1 
ATOM   1424 C  CG  . TRP   A 1 190 ? 12.706 -20.798 45.217  1.00 38.82  ? 883  TRP   A CG  1 
ATOM   1425 C  CD1 . TRP   A 1 190 ? 13.856 -20.119 44.948  1.00 39.28  ? 883  TRP   A CD1 1 
ATOM   1426 C  CD2 . TRP   A 1 190 ? 12.963 -21.580 46.391  1.00 38.27  ? 883  TRP   A CD2 1 
ATOM   1427 N  NE1 . TRP   A 1 190 ? 14.807 -20.412 45.896  1.00 39.40  ? 883  TRP   A NE1 1 
ATOM   1428 C  CE2 . TRP   A 1 190 ? 14.281 -21.305 46.796  1.00 38.88  ? 883  TRP   A CE2 1 
ATOM   1429 C  CE3 . TRP   A 1 190 ? 12.213 -22.512 47.120  1.00 38.64  ? 883  TRP   A CE3 1 
ATOM   1430 C  CZ2 . TRP   A 1 190 ? 14.859 -21.919 47.899  1.00 39.51  ? 883  TRP   A CZ2 1 
ATOM   1431 C  CZ3 . TRP   A 1 190 ? 12.772 -23.095 48.234  1.00 39.34  ? 883  TRP   A CZ3 1 
ATOM   1432 C  CH2 . TRP   A 1 190 ? 14.090 -22.819 48.599  1.00 39.66  ? 883  TRP   A CH2 1 
ATOM   1433 N  N   . MET   A 1 191 ? 8.081  -19.843 44.076  1.00 40.32  ? 884  MET   A N   1 
ATOM   1434 C  CA  . MET   A 1 191 ? 7.065  -19.596 43.070  1.00 40.63  ? 884  MET   A CA  1 
ATOM   1435 C  C   . MET   A 1 191 ? 6.318  -18.306 43.247  1.00 41.24  ? 884  MET   A C   1 
ATOM   1436 O  O   . MET   A 1 191 ? 6.018  -17.890 44.366  1.00 41.92  ? 884  MET   A O   1 
ATOM   1437 C  CB  . MET   A 1 191 ? 6.061  -20.745 43.046  1.00 40.88  ? 884  MET   A CB  1 
ATOM   1438 C  CG  . MET   A 1 191 ? 6.590  -21.984 42.366  1.00 41.95  ? 884  MET   A CG  1 
ATOM   1439 S  SD  . MET   A 1 191 ? 5.709  -23.455 42.916  1.00 41.47  ? 884  MET   A SD  1 
ATOM   1440 C  CE  . MET   A 1 191 ? 4.126  -23.131 42.203  1.00 41.25  ? 884  MET   A CE  1 
ATOM   1441 N  N   . ALA   A 1 192 ? 5.962  -17.704 42.123  1.00 40.93  ? 885  ALA   A N   1 
ATOM   1442 C  CA  . ALA   A 1 192 ? 5.163  -16.495 42.090  1.00 40.90  ? 885  ALA   A CA  1 
ATOM   1443 C  C   . ALA   A 1 192 ? 3.726  -16.855 42.488  1.00 41.02  ? 885  ALA   A C   1 
ATOM   1444 O  O   . ALA   A 1 192 ? 3.305  -17.991 42.292  1.00 40.87  ? 885  ALA   A O   1 
ATOM   1445 C  CB  . ALA   A 1 192 ? 5.196  -15.896 40.688  1.00 40.77  ? 885  ALA   A CB  1 
ATOM   1446 N  N   . LEU   A 1 193 ? 2.965  -15.897 43.027  1.00 41.04  ? 886  LEU   A N   1 
ATOM   1447 C  CA  . LEU   A 1 193 ? 1.584  -16.149 43.447  1.00 41.45  ? 886  LEU   A CA  1 
ATOM   1448 C  C   . LEU   A 1 193 ? 0.709  -16.754 42.345  1.00 42.60  ? 886  LEU   A C   1 
ATOM   1449 O  O   . LEU   A 1 193 ? 0.020  -17.732 42.606  1.00 43.14  ? 886  LEU   A O   1 
ATOM   1450 C  CB  . LEU   A 1 193 ? 0.939  -14.877 44.010  1.00 41.11  ? 886  LEU   A CB  1 
ATOM   1451 C  CG  . LEU   A 1 193 ? -0.367 -15.061 44.766  1.00 41.77  ? 886  LEU   A CG  1 
ATOM   1452 C  CD1 . LEU   A 1 193 ? -0.185 -15.962 45.954  1.00 41.74  ? 886  LEU   A CD1 1 
ATOM   1453 C  CD2 . LEU   A 1 193 ? -0.899 -13.736 45.234  1.00 42.56  ? 886  LEU   A CD2 1 
ATOM   1454 N  N   . GLU   A 1 194 ? 0.774  -16.228 41.111  1.00 42.50  ? 887  GLU   A N   1 
ATOM   1455 C  CA  . GLU   A 1 194 ? -0.008 -16.784 40.004  1.00 43.00  ? 887  GLU   A CA  1 
ATOM   1456 C  C   . GLU   A 1 194 ? 0.371  -18.225 39.646  1.00 44.32  ? 887  GLU   A C   1 
ATOM   1457 O  O   . GLU   A 1 194 ? -0.380 -18.887 38.930  1.00 45.03  ? 887  GLU   A O   1 
ATOM   1458 C  CB  . GLU   A 1 194 ? 0.081  -15.892 38.762  1.00 43.98  ? 887  GLU   A CB  1 
ATOM   1459 C  CG  . GLU   A 1 194 ? 1.433  -15.914 38.069  1.00 45.12  ? 887  GLU   A CG  1 
ATOM   1460 C  CD  . GLU   A 1 194 ? 2.459  -14.906 38.554  1.00 46.39  ? 887  GLU   A CD  1 
ATOM   1461 O  OE1 . GLU   A 1 194 ? 2.280  -14.328 39.651  1.00 46.43  ? 887  GLU   A OE1 1 
ATOM   1462 O  OE2 . GLU   A 1 194 ? 3.449  -14.690 37.822  1.00 47.81  ? 887  GLU   A OE2 1 
ATOM   1463 N  N   . SER   A 1 195 ? 1.540  -18.700 40.104  1.00 44.33  ? 888  SER   A N   1 
ATOM   1464 C  CA  . SER   A 1 195 ? 1.982  -20.066 39.852  1.00 44.81  ? 888  SER   A CA  1 
ATOM   1465 C  C   . SER   A 1 195 ? 1.478  -20.971 40.965  1.00 46.01  ? 888  SER   A C   1 
ATOM   1466 O  O   . SER   A 1 195 ? 1.093  -22.095 40.684  1.00 46.96  ? 888  SER   A O   1 
ATOM   1467 C  CB  . SER   A 1 195 ? 3.501  -20.138 39.761  1.00 44.88  ? 888  SER   A CB  1 
ATOM   1468 O  OG  . SER   A 1 195 ? 3.976  -19.350 38.685  1.00 45.14  ? 888  SER   A OG  1 
ATOM   1469 N  N   . ILE   A 1 196 ? 1.476  -20.495 42.221  1.00 46.14  ? 889  ILE   A N   1 
ATOM   1470 C  CA  . ILE   A 1 196 ? 0.963  -21.234 43.375  1.00 46.87  ? 889  ILE   A CA  1 
ATOM   1471 C  C   . ILE   A 1 196 ? -0.553 -21.399 43.217  1.00 48.40  ? 889  ILE   A C   1 
ATOM   1472 O  O   . ILE   A 1 196 ? -1.081 -22.495 43.394  1.00 49.21  ? 889  ILE   A O   1 
ATOM   1473 C  CB  . ILE   A 1 196 ? 1.292  -20.495 44.702  1.00 46.79  ? 889  ILE   A CB  1 
ATOM   1474 C  CG1 . ILE   A 1 196 ? 2.802  -20.457 44.973  1.00 47.36  ? 889  ILE   A CG1 1 
ATOM   1475 C  CG2 . ILE   A 1 196 ? 0.540  -21.109 45.880  1.00 47.31  ? 889  ILE   A CG2 1 
ATOM   1476 C  CD1 . ILE   A 1 196 ? 3.184  -19.520 46.101  1.00 48.25  ? 889  ILE   A CD1 1 
ATOM   1477 N  N   . LEU   A 1 197 ? -1.245 -20.319 42.856  1.00 48.74  ? 890  LEU   A N   1 
ATOM   1478 C  CA  . LEU   A 1 197 ? -2.684 -20.342 42.707  1.00 49.51  ? 890  LEU   A CA  1 
ATOM   1479 C  C   . LEU   A 1 197 ? -3.193 -20.978 41.438  1.00 50.81  ? 890  LEU   A C   1 
ATOM   1480 O  O   . LEU   A 1 197 ? -4.121 -21.783 41.517  1.00 51.39  ? 890  LEU   A O   1 
ATOM   1481 C  CB  . LEU   A 1 197 ? -3.273 -18.930 42.836  1.00 49.43  ? 890  LEU   A CB  1 
ATOM   1482 C  CG  . LEU   A 1 197 ? -3.002 -18.168 44.124  1.00 50.39  ? 890  LEU   A CG  1 
ATOM   1483 C  CD1 . LEU   A 1 197 ? -3.749 -16.868 44.121  1.00 50.88  ? 890  LEU   A CD1 1 
ATOM   1484 C  CD2 . LEU   A 1 197 ? -3.394 -18.971 45.354  1.00 50.84  ? 890  LEU   A CD2 1 
ATOM   1485 N  N   . HIS   A 1 198 ? -2.648 -20.604 40.271  1.00 51.30  ? 891  HIS   A N   1 
ATOM   1486 C  CA  . HIS   A 1 198 ? -3.221 -21.067 39.011  1.00 52.31  ? 891  HIS   A CA  1 
ATOM   1487 C  C   . HIS   A 1 198 ? -2.297 -21.840 38.103  1.00 52.71  ? 891  HIS   A C   1 
ATOM   1488 O  O   . HIS   A 1 198 ? -2.663 -22.062 36.952  1.00 52.90  ? 891  HIS   A O   1 
ATOM   1489 C  CB  . HIS   A 1 198 ? -3.825 -19.877 38.244  1.00 53.81  ? 891  HIS   A CB  1 
ATOM   1490 C  CG  . HIS   A 1 198 ? -4.725 -19.035 39.095  1.00 57.30  ? 891  HIS   A CG  1 
ATOM   1491 N  ND1 . HIS   A 1 198 ? -4.345 -17.770 39.515  1.00 59.43  ? 891  HIS   A ND1 1 
ATOM   1492 C  CD2 . HIS   A 1 198 ? -5.901 -19.355 39.683  1.00 58.75  ? 891  HIS   A CD2 1 
ATOM   1493 C  CE1 . HIS   A 1 198 ? -5.329 -17.335 40.283  1.00 59.95  ? 891  HIS   A CE1 1 
ATOM   1494 N  NE2 . HIS   A 1 198 ? -6.285 -18.258 40.420  1.00 60.08  ? 891  HIS   A NE2 1 
ATOM   1495 N  N   . ARG   A 1 199 ? -1.134 -22.266 38.592  1.00 52.87  ? 892  ARG   A N   1 
ATOM   1496 C  CA  . ARG   A 1 199 ? -0.165 -23.014 37.795  1.00 53.88  ? 892  ARG   A CA  1 
ATOM   1497 C  C   . ARG   A 1 199 ? 0.203  -22.308 36.476  1.00 54.70  ? 892  ARG   A C   1 
ATOM   1498 O  O   . ARG   A 1 199 ? 0.335  -22.957 35.433  1.00 55.25  ? 892  ARG   A O   1 
ATOM   1499 C  CB  . ARG   A 1 199 ? -0.618 -24.461 37.562  1.00 55.93  ? 892  ARG   A CB  1 
ATOM   1500 C  CG  . ARG   A 1 199 ? -0.475 -25.362 38.791  1.00 61.34  ? 892  ARG   A CG  1 
ATOM   1501 C  CD  . ARG   A 1 199 ? 0.983  -25.524 39.229  1.00 66.31  ? 892  ARG   A CD  1 
ATOM   1502 N  NE  . ARG   A 1 199 ? 1.146  -26.412 40.385  1.00 70.28  ? 892  ARG   A NE  1 
ATOM   1503 C  CZ  . ARG   A 1 199 ? 1.063  -26.017 41.655  1.00 72.74  ? 892  ARG   A CZ  1 
ATOM   1504 N  NH1 . ARG   A 1 199 ? 0.809  -24.751 41.949  1.00 71.59  ? 892  ARG   A NH1 1 
ATOM   1505 N  NH2 . ARG   A 1 199 ? 1.227  -26.891 42.641  1.00 73.45  ? 892  ARG   A NH2 1 
ATOM   1506 N  N   . ILE   A 1 200 ? 0.318  -20.966 36.526  1.00 54.36  ? 893  ILE   A N   1 
ATOM   1507 C  CA  . ILE   A 1 200 ? 0.693  -20.130 35.384  1.00 54.14  ? 893  ILE   A CA  1 
ATOM   1508 C  C   . ILE   A 1 200 ? 2.200  -19.881 35.466  1.00 53.54  ? 893  ILE   A C   1 
ATOM   1509 O  O   . ILE   A 1 200 ? 2.681  -19.337 36.472  1.00 53.88  ? 893  ILE   A O   1 
ATOM   1510 C  CB  . ILE   A 1 200 ? -0.082 -18.786 35.416  1.00 54.67  ? 893  ILE   A CB  1 
ATOM   1511 C  CG1 . ILE   A 1 200 ? -1.589 -19.015 35.253  1.00 55.98  ? 893  ILE   A CG1 1 
ATOM   1512 C  CG2 . ILE   A 1 200 ? 0.463  -17.790 34.382  1.00 54.66  ? 893  ILE   A CG2 1 
ATOM   1513 C  CD1 . ILE   A 1 200 ? -2.404 -17.801 35.561  1.00 57.58  ? 893  ILE   A CD1 1 
ATOM   1514 N  N   . TYR   A 1 201 ? 2.948  -20.301 34.443  1.00 52.36  ? 894  TYR   A N   1 
ATOM   1515 C  CA  . TYR   A 1 201 ? 4.393  -20.107 34.456  1.00 51.89  ? 894  TYR   A CA  1 
ATOM   1516 C  C   . TYR   A 1 201 ? 4.885  -19.310 33.249  1.00 51.37  ? 894  TYR   A C   1 
ATOM   1517 O  O   . TYR   A 1 201 ? 4.815  -19.791 32.123  1.00 51.90  ? 894  TYR   A O   1 
ATOM   1518 C  CB  . TYR   A 1 201 ? 5.123  -21.444 34.573  1.00 51.80  ? 894  TYR   A CB  1 
ATOM   1519 C  CG  . TYR   A 1 201 ? 4.871  -22.203 35.864  1.00 52.23  ? 894  TYR   A CG  1 
ATOM   1520 C  CD1 . TYR   A 1 201 ? 3.741  -22.991 36.020  1.00 53.06  ? 894  TYR   A CD1 1 
ATOM   1521 C  CD2 . TYR   A 1 201 ? 5.823  -22.230 36.872  1.00 52.85  ? 894  TYR   A CD2 1 
ATOM   1522 C  CE1 . TYR   A 1 201 ? 3.543  -23.754 37.161  1.00 53.91  ? 894  TYR   A CE1 1 
ATOM   1523 C  CE2 . TYR   A 1 201 ? 5.633  -22.983 38.022  1.00 53.88  ? 894  TYR   A CE2 1 
ATOM   1524 C  CZ  . TYR   A 1 201 ? 4.492  -23.753 38.161  1.00 54.92  ? 894  TYR   A CZ  1 
ATOM   1525 O  OH  . TYR   A 1 201 ? 4.297  -24.530 39.283  1.00 56.46  ? 894  TYR   A OH  1 
ATOM   1526 N  N   . THR   A 1 202 ? 5.356  -18.078 33.483  1.00 50.13  ? 895  THR   A N   1 
ATOM   1527 C  CA  . THR   A 1 202 ? 5.866  -17.190 32.441  1.00 49.72  ? 895  THR   A CA  1 
ATOM   1528 C  C   . THR   A 1 202 ? 7.309  -16.738 32.776  1.00 48.79  ? 895  THR   A C   1 
ATOM   1529 O  O   . THR   A 1 202 ? 7.821  -17.058 33.853  1.00 48.97  ? 895  THR   A O   1 
ATOM   1530 C  CB  . THR   A 1 202 ? 4.915  -15.972 32.300  1.00 51.48  ? 895  THR   A CB  1 
ATOM   1531 O  OG1 . THR   A 1 202 ? 5.030  -15.134 33.457  1.00 52.84  ? 895  THR   A OG1 1 
ATOM   1532 C  CG2 . THR   A 1 202 ? 3.471  -16.381 32.065  1.00 52.03  ? 895  THR   A CG2 1 
ATOM   1533 N  N   . HIS   A 1 203 ? 7.958  -15.963 31.877  1.00 47.38  ? 896  HIS   A N   1 
ATOM   1534 C  CA  . HIS   A 1 203 ? 9.273  -15.397 32.167  1.00 46.24  ? 896  HIS   A CA  1 
ATOM   1535 C  C   . HIS   A 1 203 ? 9.213  -14.467 33.384  1.00 45.67  ? 896  HIS   A C   1 
ATOM   1536 O  O   . HIS   A 1 203 ? 10.193 -14.359 34.111  1.00 46.30  ? 896  HIS   A O   1 
ATOM   1537 C  CB  . HIS   A 1 203 ? 9.804  -14.635 30.957  1.00 46.10  ? 896  HIS   A CB  1 
ATOM   1538 C  CG  . HIS   A 1 203 ? 10.003 -15.513 29.766  1.00 46.73  ? 896  HIS   A CG  1 
ATOM   1539 N  ND1 . HIS   A 1 203 ? 9.275  -15.329 28.608  1.00 48.15  ? 896  HIS   A ND1 1 
ATOM   1540 C  CD2 . HIS   A 1 203 ? 10.817 -16.578 29.609  1.00 47.32  ? 896  HIS   A CD2 1 
ATOM   1541 C  CE1 . HIS   A 1 203 ? 9.691  -16.264 27.774  1.00 48.61  ? 896  HIS   A CE1 1 
ATOM   1542 N  NE2 . HIS   A 1 203 ? 10.612 -17.044 28.337  1.00 48.58  ? 896  HIS   A NE2 1 
ATOM   1543 N  N   . GLN   A 1 204 ? 8.052  -13.834 33.635  1.00 44.40  ? 897  GLN   A N   1 
ATOM   1544 C  CA  . GLN   A 1 204 ? 7.845  -12.942 34.772  1.00 43.21  ? 897  GLN   A CA  1 
ATOM   1545 C  C   . GLN   A 1 204 ? 7.688  -13.696 36.080  1.00 41.57  ? 897  GLN   A C   1 
ATOM   1546 O  O   . GLN   A 1 204 ? 8.056  -13.168 37.129  1.00 41.44  ? 897  GLN   A O   1 
ATOM   1547 C  CB  . GLN   A 1 204 ? 6.693  -11.976 34.502  1.00 44.63  ? 897  GLN   A CB  1 
ATOM   1548 C  CG  . GLN   A 1 204 ? 6.971  -11.073 33.285  1.00 47.17  ? 897  GLN   A CG  1 
ATOM   1549 C  CD  . GLN   A 1 204 ? 8.288  -10.311 33.367  1.00 50.22  ? 897  GLN   A CD  1 
ATOM   1550 O  OE1 . GLN   A 1 204 ? 8.483  -9.459  34.236  1.00 51.80  ? 897  GLN   A OE1 1 
ATOM   1551 N  NE2 . GLN   A 1 204 ? 9.224  -10.598 32.460  1.00 50.38  ? 897  GLN   A NE2 1 
ATOM   1552 N  N   . SER   A 1 205 ? 7.204  -14.940 36.027  1.00 40.24  ? 898  SER   A N   1 
ATOM   1553 C  CA  . SER   A 1 205 ? 7.188  -15.799 37.204  1.00 39.94  ? 898  SER   A CA  1 
ATOM   1554 C  C   . SER   A 1 205 ? 8.663  -16.241 37.510  1.00 39.56  ? 898  SER   A C   1 
ATOM   1555 O  O   . SER   A 1 205 ? 9.038  -16.399 38.673  1.00 39.87  ? 898  SER   A O   1 
ATOM   1556 C  CB  . SER   A 1 205 ? 6.267  -17.000 36.997  1.00 40.90  ? 898  SER   A CB  1 
ATOM   1557 O  OG  . SER   A 1 205 ? 6.788  -17.932 36.063  1.00 43.54  ? 898  SER   A OG  1 
ATOM   1558 N  N   . ASP   A 1 206 ? 9.508  -16.377 36.464  1.00 38.59  ? 899  ASP   A N   1 
ATOM   1559 C  CA  . ASP   A 1 206 ? 10.924 -16.683 36.586  1.00 37.61  ? 899  ASP   A CA  1 
ATOM   1560 C  C   . ASP   A 1 206 ? 11.642 -15.535 37.271  1.00 36.71  ? 899  ASP   A C   1 
ATOM   1561 O  O   . ASP   A 1 206 ? 12.564 -15.794 38.035  1.00 37.01  ? 899  ASP   A O   1 
ATOM   1562 C  CB  . ASP   A 1 206 ? 11.533 -16.930 35.207  1.00 38.93  ? 899  ASP   A CB  1 
ATOM   1563 C  CG  . ASP   A 1 206 ? 11.387 -18.343 34.682  1.00 41.94  ? 899  ASP   A CG  1 
ATOM   1564 O  OD1 . ASP   A 1 206 ? 10.884 -19.213 35.435  1.00 41.55  ? 899  ASP   A OD1 1 
ATOM   1565 O  OD2 . ASP   A 1 206 ? 11.791 -18.587 33.522  1.00 43.97  ? 899  ASP   A OD2 1 
ATOM   1566 N  N   . VAL   A 1 207 ? 11.220 -14.274 37.023  1.00 35.86  ? 900  VAL   A N   1 
ATOM   1567 C  CA  . VAL   A 1 207 ? 11.773 -13.094 37.683  1.00 35.84  ? 900  VAL   A CA  1 
ATOM   1568 C  C   . VAL   A 1 207 ? 11.494 -13.194 39.185  1.00 37.20  ? 900  VAL   A C   1 
ATOM   1569 O  O   . VAL   A 1 207 ? 12.400 -12.943 39.986  1.00 37.46  ? 900  VAL   A O   1 
ATOM   1570 C  CB  . VAL   A 1 207 ? 11.233 -11.771 37.106  1.00 35.73  ? 900  VAL   A CB  1 
ATOM   1571 C  CG1 . VAL   A 1 207 ? 11.866 -10.584 37.809  1.00 36.09  ? 900  VAL   A CG1 1 
ATOM   1572 C  CG2 . VAL   A 1 207 ? 11.486 -11.683 35.613  1.00 36.05  ? 900  VAL   A CG2 1 
ATOM   1573 N  N   . TRP   A 1 208 ? 10.279 -13.666 39.586  1.00 37.53  ? 901  TRP   A N   1 
ATOM   1574 C  CA  . TRP   A 1 208 ? 9.942  -13.862 41.001  1.00 37.95  ? 901  TRP   A CA  1 
ATOM   1575 C  C   . TRP   A 1 208 ? 10.958 -14.775 41.671  1.00 38.58  ? 901  TRP   A C   1 
ATOM   1576 O  O   . TRP   A 1 208 ? 11.543 -14.386 42.685  1.00 39.35  ? 901  TRP   A O   1 
ATOM   1577 C  CB  . TRP   A 1 208 ? 8.523  -14.438 41.195  1.00 38.05  ? 901  TRP   A CB  1 
ATOM   1578 C  CG  . TRP   A 1 208 ? 8.136  -14.541 42.643  1.00 38.75  ? 901  TRP   A CG  1 
ATOM   1579 C  CD1 . TRP   A 1 208 ? 8.766  -15.263 43.611  1.00 39.83  ? 901  TRP   A CD1 1 
ATOM   1580 C  CD2 . TRP   A 1 208 ? 7.081  -13.829 43.299  1.00 38.89  ? 901  TRP   A CD2 1 
ATOM   1581 N  NE1 . TRP   A 1 208 ? 8.172  -15.043 44.830  1.00 40.39  ? 901  TRP   A NE1 1 
ATOM   1582 C  CE2 . TRP   A 1 208 ? 7.119  -14.184 44.663  1.00 39.93  ? 901  TRP   A CE2 1 
ATOM   1583 C  CE3 . TRP   A 1 208 ? 6.067  -12.979 42.857  1.00 39.34  ? 901  TRP   A CE3 1 
ATOM   1584 C  CZ2 . TRP   A 1 208 ? 6.208  -13.687 45.589  1.00 40.44  ? 901  TRP   A CZ2 1 
ATOM   1585 C  CZ3 . TRP   A 1 208 ? 5.164  -12.492 43.778  1.00 40.35  ? 901  TRP   A CZ3 1 
ATOM   1586 C  CH2 . TRP   A 1 208 ? 5.231  -12.857 45.122  1.00 40.55  ? 901  TRP   A CH2 1 
ATOM   1587 N  N   . SER   A 1 209 ? 11.218 -15.952 41.052  1.00 38.19  ? 902  SER   A N   1 
ATOM   1588 C  CA  . SER   A 1 209 ? 12.182 -16.958 41.513  1.00 37.91  ? 902  SER   A CA  1 
ATOM   1589 C  C   . SER   A 1 209 ? 13.599 -16.406 41.506  1.00 37.41  ? 902  SER   A C   1 
ATOM   1590 O  O   . SER   A 1 209 ? 14.373 -16.749 42.389  1.00 37.92  ? 902  SER   A O   1 
ATOM   1591 C  CB  . SER   A 1 209 ? 12.102 -18.199 40.645  1.00 39.08  ? 902  SER   A CB  1 
ATOM   1592 O  OG  . SER   A 1 209 ? 10.756 -18.636 40.543  1.00 41.34  ? 902  SER   A OG  1 
ATOM   1593 N  N   . TYR   A 1 210 ? 13.921 -15.515 40.551  1.00 36.29  ? 903  TYR   A N   1 
ATOM   1594 C  CA  . TYR   A 1 210 ? 15.205 -14.834 40.466  1.00 35.95  ? 903  TYR   A CA  1 
ATOM   1595 C  C   . TYR   A 1 210 ? 15.400 -13.954 41.690  1.00 36.69  ? 903  TYR   A C   1 
ATOM   1596 O  O   . TYR   A 1 210 ? 16.489 -13.952 42.246  1.00 37.63  ? 903  TYR   A O   1 
ATOM   1597 C  CB  . TYR   A 1 210 ? 15.330 -14.021 39.161  1.00 35.24  ? 903  TYR   A CB  1 
ATOM   1598 C  CG  . TYR   A 1 210 ? 16.562 -13.141 39.105  1.00 34.42  ? 903  TYR   A CG  1 
ATOM   1599 C  CD1 . TYR   A 1 210 ? 17.786 -13.649 38.702  1.00 34.18  ? 903  TYR   A CD1 1 
ATOM   1600 C  CD2 . TYR   A 1 210 ? 16.505 -11.804 39.484  1.00 34.57  ? 903  TYR   A CD2 1 
ATOM   1601 C  CE1 . TYR   A 1 210 ? 18.925 -12.851 38.681  1.00 34.58  ? 903  TYR   A CE1 1 
ATOM   1602 C  CE2 . TYR   A 1 210 ? 17.637 -10.999 39.470  1.00 34.71  ? 903  TYR   A CE2 1 
ATOM   1603 C  CZ  . TYR   A 1 210 ? 18.843 -11.522 39.054  1.00 35.22  ? 903  TYR   A CZ  1 
ATOM   1604 O  OH  . TYR   A 1 210 ? 19.959 -10.723 39.041  1.00 36.18  ? 903  TYR   A OH  1 
ATOM   1605 N  N   . GLY   A 1 211 ? 14.355 -13.246 42.121  1.00 36.12  ? 904  GLY   A N   1 
ATOM   1606 C  CA  . GLY   A 1 211 ? 14.420 -12.413 43.316  1.00 35.73  ? 904  GLY   A CA  1 
ATOM   1607 C  C   . GLY   A 1 211 ? 14.679 -13.244 44.560  1.00 35.57  ? 904  GLY   A C   1 
ATOM   1608 O  O   . GLY   A 1 211 ? 15.454 -12.854 45.439  1.00 35.45  ? 904  GLY   A O   1 
ATOM   1609 N  N   . VAL   A 1 212 ? 14.061 -14.424 44.626  1.00 35.29  ? 905  VAL   A N   1 
ATOM   1610 C  CA  . VAL   A 1 212 ? 14.254 -15.332 45.754  1.00 34.84  ? 905  VAL   A CA  1 
ATOM   1611 C  C   . VAL   A 1 212 ? 15.689 -15.851 45.739  1.00 34.77  ? 905  VAL   A C   1 
ATOM   1612 O  O   . VAL   A 1 212 ? 16.322 -15.868 46.792  1.00 35.63  ? 905  VAL   A O   1 
ATOM   1613 C  CB  . VAL   A 1 212 ? 13.233 -16.488 45.763  1.00 34.49  ? 905  VAL   A CB  1 
ATOM   1614 C  CG1 . VAL   A 1 212 ? 13.364 -17.299 47.039  1.00 34.68  ? 905  VAL   A CG1 1 
ATOM   1615 C  CG2 . VAL   A 1 212 ? 11.810 -15.969 45.601  1.00 34.33  ? 905  VAL   A CG2 1 
ATOM   1616 N  N   . THR   A 1 213 ? 16.214 -16.214 44.538  1.00 33.14  ? 906  THR   A N   1 
ATOM   1617 C  CA  . THR   A 1 213 ? 17.574 -16.710 44.309  1.00 32.33  ? 906  THR   A CA  1 
ATOM   1618 C  C   . THR   A 1 213 ? 18.582 -15.666 44.762  1.00 32.22  ? 906  THR   A C   1 
ATOM   1619 O  O   . THR   A 1 213 ? 19.545 -15.997 45.437  1.00 32.11  ? 906  THR   A O   1 
ATOM   1620 C  CB  . THR   A 1 213 ? 17.752 -17.048 42.818  1.00 33.14  ? 906  THR   A CB  1 
ATOM   1621 O  OG1 . THR   A 1 213 ? 16.826 -18.065 42.450  1.00 33.78  ? 906  THR   A OG1 1 
ATOM   1622 C  CG2 . THR   A 1 213 ? 19.150 -17.495 42.475  1.00 33.18  ? 906  THR   A CG2 1 
ATOM   1623 N  N   . VAL   A 1 214 ? 18.337 -14.400 44.435  1.00 32.35  ? 907  VAL   A N   1 
ATOM   1624 C  CA  . VAL   A 1 214 ? 19.189 -13.291 44.844  1.00 32.99  ? 907  VAL   A CA  1 
ATOM   1625 C  C   . VAL   A 1 214 ? 19.177 -13.162 46.366  1.00 34.23  ? 907  VAL   A C   1 
ATOM   1626 O  O   . VAL   A 1 214 ? 20.241 -13.078 46.964  1.00 34.93  ? 907  VAL   A O   1 
ATOM   1627 C  CB  . VAL   A 1 214 ? 18.775 -11.993 44.118  1.00 33.11  ? 907  VAL   A CB  1 
ATOM   1628 C  CG1 . VAL   A 1 214 ? 19.359 -10.754 44.796  1.00 33.71  ? 907  VAL   A CG1 1 
ATOM   1629 C  CG2 . VAL   A 1 214 ? 19.176 -12.051 42.650  1.00 32.95  ? 907  VAL   A CG2 1 
ATOM   1630 N  N   . TRP   A 1 215 ? 17.994 -13.248 46.996  1.00 34.42  ? 908  TRP   A N   1 
ATOM   1631 C  CA  . TRP   A 1 215 ? 17.856 -13.210 48.451  1.00 35.14  ? 908  TRP   A CA  1 
ATOM   1632 C  C   . TRP   A 1 215 ? 18.633 -14.360 49.110  1.00 36.10  ? 908  TRP   A C   1 
ATOM   1633 O  O   . TRP   A 1 215 ? 19.308 -14.143 50.109  1.00 36.86  ? 908  TRP   A O   1 
ATOM   1634 C  CB  . TRP   A 1 215 ? 16.375 -13.249 48.856  1.00 35.02  ? 908  TRP   A CB  1 
ATOM   1635 C  CG  . TRP   A 1 215 ? 16.131 -13.124 50.338  1.00 35.36  ? 908  TRP   A CG  1 
ATOM   1636 C  CD1 . TRP   A 1 215 ? 15.934 -11.974 51.046  1.00 35.89  ? 908  TRP   A CD1 1 
ATOM   1637 C  CD2 . TRP   A 1 215 ? 16.036 -14.202 51.287  1.00 35.46  ? 908  TRP   A CD2 1 
ATOM   1638 N  NE1 . TRP   A 1 215 ? 15.745 -12.263 52.378  1.00 36.15  ? 908  TRP   A NE1 1 
ATOM   1639 C  CE2 . TRP   A 1 215 ? 15.816 -13.622 52.557  1.00 36.08  ? 908  TRP   A CE2 1 
ATOM   1640 C  CE3 . TRP   A 1 215 ? 16.146 -15.602 51.188  1.00 35.67  ? 908  TRP   A CE3 1 
ATOM   1641 C  CZ2 . TRP   A 1 215 ? 15.670 -14.392 53.712  1.00 36.66  ? 908  TRP   A CZ2 1 
ATOM   1642 C  CZ3 . TRP   A 1 215 ? 16.017 -16.359 52.333  1.00 36.54  ? 908  TRP   A CZ3 1 
ATOM   1643 C  CH2 . TRP   A 1 215 ? 15.760 -15.758 53.575  1.00 36.91  ? 908  TRP   A CH2 1 
ATOM   1644 N  N   . GLU   A 1 216 ? 18.591 -15.566 48.532  1.00 36.04  ? 909  GLU   A N   1 
ATOM   1645 C  CA  . GLU   A 1 216 ? 19.354 -16.707 49.050  1.00 36.72  ? 909  GLU   A CA  1 
ATOM   1646 C  C   . GLU   A 1 216 ? 20.857 -16.381 49.064  1.00 37.51  ? 909  GLU   A C   1 
ATOM   1647 O  O   . GLU   A 1 216 ? 21.545 -16.754 50.000  1.00 38.02  ? 909  GLU   A O   1 
ATOM   1648 C  CB  . GLU   A 1 216 ? 19.150 -17.952 48.177  1.00 37.43  ? 909  GLU   A CB  1 
ATOM   1649 C  CG  . GLU   A 1 216 ? 17.782 -18.594 48.251  1.00 39.58  ? 909  GLU   A CG  1 
ATOM   1650 C  CD  . GLU   A 1 216 ? 17.715 -19.886 47.449  1.00 42.07  ? 909  GLU   A CD  1 
ATOM   1651 O  OE1 . GLU   A 1 216 ? 17.287 -19.840 46.273  1.00 39.74  ? 909  GLU   A OE1 1 
ATOM   1652 O  OE2 . GLU   A 1 216 ? 18.106 -20.945 47.993  1.00 43.78  ? 909  GLU   A OE2 1 
ATOM   1653 N  N   . LEU   A 1 217 ? 21.350 -15.682 48.035  1.00 37.20  ? 910  LEU   A N   1 
ATOM   1654 C  CA  . LEU   A 1 217 ? 22.754 -15.309 47.948  1.00 37.51  ? 910  LEU   A CA  1 
ATOM   1655 C  C   . LEU   A 1 217 ? 23.099 -14.239 48.978  1.00 38.27  ? 910  LEU   A C   1 
ATOM   1656 O  O   . LEU   A 1 217 ? 24.101 -14.370 49.677  1.00 38.68  ? 910  LEU   A O   1 
ATOM   1657 C  CB  . LEU   A 1 217 ? 23.110 -14.802 46.527  1.00 37.06  ? 910  LEU   A CB  1 
ATOM   1658 C  CG  . LEU   A 1 217 ? 22.790 -15.720 45.367  1.00 37.87  ? 910  LEU   A CG  1 
ATOM   1659 C  CD1 . LEU   A 1 217 ? 23.278 -15.114 44.041  1.00 38.73  ? 910  LEU   A CD1 1 
ATOM   1660 C  CD2 . LEU   A 1 217 ? 23.374 -17.094 45.568  1.00 37.63  ? 910  LEU   A CD2 1 
ATOM   1661 N  N   . MET   A 1 218 ? 22.268 -13.192 49.083  1.00 38.08  ? 911  MET   A N   1 
ATOM   1662 C  CA  . MET   A 1 218 ? 22.490 -12.100 50.028  1.00 38.48  ? 911  MET   A CA  1 
ATOM   1663 C  C   . MET   A 1 218 ? 22.419 -12.545 51.493  1.00 38.77  ? 911  MET   A C   1 
ATOM   1664 O  O   . MET   A 1 218 ? 23.039 -11.919 52.353  1.00 39.15  ? 911  MET   A O   1 
ATOM   1665 C  CB  . MET   A 1 218 ? 21.515 -10.955 49.761  1.00 38.49  ? 911  MET   A CB  1 
ATOM   1666 C  CG  . MET   A 1 218 ? 21.591 -10.436 48.370  1.00 39.84  ? 911  MET   A CG  1 
ATOM   1667 S  SD  . MET   A 1 218 ? 23.207 -9.748  47.965  1.00 42.58  ? 911  MET   A SD  1 
ATOM   1668 C  CE  . MET   A 1 218 ? 22.994 -9.472  46.165  1.00 28.00  ? 911  MET   A CE  1 
ATOM   1669 N  N   . THR   A 1 219 ? 21.665 -13.613 51.774  1.00 38.39  ? 912  THR   A N   1 
ATOM   1670 C  CA  . THR   A 1 219 ? 21.572 -14.166 53.117  1.00 38.83  ? 912  THR   A CA  1 
ATOM   1671 C  C   . THR   A 1 219 ? 22.589 -15.297 53.360  1.00 39.79  ? 912  THR   A C   1 
ATOM   1672 O  O   . THR   A 1 219 ? 22.543 -15.909 54.423  1.00 40.66  ? 912  THR   A O   1 
ATOM   1673 C  CB  . THR   A 1 219 ? 20.152 -14.653 53.403  1.00 39.66  ? 912  THR   A CB  1 
ATOM   1674 O  OG1 . THR   A 1 219 ? 19.782 -15.628 52.428  1.00 40.73  ? 912  THR   A OG1 1 
ATOM   1675 C  CG2 . THR   A 1 219 ? 19.145 -13.520 53.436  1.00 39.77  ? 912  THR   A CG2 1 
ATOM   1676 N  N   . PHE   A 1 220 ? 23.485 -15.584 52.387  1.00 39.54  ? 913  PHE   A N   1 
ATOM   1677 C  CA  . PHE   A 1 220 ? 24.500 -16.631 52.423  1.00 39.44  ? 913  PHE   A CA  1 
ATOM   1678 C  C   . PHE   A 1 220 ? 23.924 -18.027 52.611  1.00 40.97  ? 913  PHE   A C   1 
ATOM   1679 O  O   . PHE   A 1 220 ? 24.447 -18.836 53.388  1.00 41.94  ? 913  PHE   A O   1 
ATOM   1680 C  CB  . PHE   A 1 220 ? 25.583 -16.332 53.444  1.00 38.54  ? 913  PHE   A CB  1 
ATOM   1681 C  CG  . PHE   A 1 220 ? 26.313 -15.037 53.170  1.00 38.33  ? 913  PHE   A CG  1 
ATOM   1682 C  CD1 . PHE   A 1 220 ? 27.291 -14.968 52.193  1.00 38.34  ? 913  PHE   A CD1 1 
ATOM   1683 C  CD2 . PHE   A 1 220 ? 26.032 -13.893 53.903  1.00 38.35  ? 913  PHE   A CD2 1 
ATOM   1684 C  CE1 . PHE   A 1 220 ? 27.970 -13.783 51.953  1.00 38.83  ? 913  PHE   A CE1 1 
ATOM   1685 C  CE2 . PHE   A 1 220 ? 26.716 -12.711 53.662  1.00 38.73  ? 913  PHE   A CE2 1 
ATOM   1686 C  CZ  . PHE   A 1 220 ? 27.679 -12.662 52.689  1.00 38.68  ? 913  PHE   A CZ  1 
ATOM   1687 N  N   . GLY   A 1 221 ? 22.852 -18.301 51.886  1.00 41.19  ? 914  GLY   A N   1 
ATOM   1688 C  CA  . GLY   A 1 221 ? 22.225 -19.612 51.865  1.00 42.14  ? 914  GLY   A CA  1 
ATOM   1689 C  C   . GLY   A 1 221 ? 21.107 -19.870 52.847  1.00 42.90  ? 914  GLY   A C   1 
ATOM   1690 O  O   . GLY   A 1 221 ? 20.905 -21.022 53.256  1.00 43.24  ? 914  GLY   A O   1 
ATOM   1691 N  N   . SER   A 1 222 ? 20.358 -18.831 53.222  1.00 43.37  ? 915  SER   A N   1 
ATOM   1692 C  CA  . SER   A 1 222 ? 19.255 -19.022 54.165  1.00 44.40  ? 915  SER   A CA  1 
ATOM   1693 C  C   . SER   A 1 222 ? 18.028 -19.630 53.491  1.00 45.39  ? 915  SER   A C   1 
ATOM   1694 O  O   . SER   A 1 222 ? 17.848 -19.491 52.279  1.00 45.39  ? 915  SER   A O   1 
ATOM   1695 C  CB  . SER   A 1 222 ? 18.915 -17.725 54.886  1.00 45.59  ? 915  SER   A CB  1 
ATOM   1696 O  OG  . SER   A 1 222 ? 19.993 -17.337 55.720  1.00 47.85  ? 915  SER   A OG  1 
ATOM   1697 N  N   . LYS   A 1 223 ? 17.214 -20.352 54.264  1.00 46.04  ? 916  LYS   A N   1 
ATOM   1698 C  CA  . LYS   A 1 223 ? 16.005 -20.967 53.736  1.00 47.07  ? 916  LYS   A CA  1 
ATOM   1699 C  C   . LYS   A 1 223 ? 14.904 -19.923 53.705  1.00 47.27  ? 916  LYS   A C   1 
ATOM   1700 O  O   . LYS   A 1 223 ? 14.623 -19.311 54.729  1.00 46.99  ? 916  LYS   A O   1 
ATOM   1701 C  CB  . LYS   A 1 223 ? 15.584 -22.168 54.603  1.00 49.62  ? 916  LYS   A CB  1 
ATOM   1702 C  CG  . LYS   A 1 223 ? 16.331 -23.457 54.259  1.00 55.03  ? 916  LYS   A CG  1 
ATOM   1703 C  CD  . LYS   A 1 223 ? 16.350 -24.438 55.415  1.00 60.60  ? 916  LYS   A CD  1 
ATOM   1704 C  CE  . LYS   A 1 223 ? 17.687 -24.453 56.128  1.00 65.91  ? 916  LYS   A CE  1 
ATOM   1705 N  NZ  . LYS   A 1 223 ? 18.014 -23.149 56.787  1.00 68.90  ? 916  LYS   A NZ  1 
ATOM   1706 N  N   . PRO   A 1 224 ? 14.287 -19.679 52.535  1.00 47.74  ? 917  PRO   A N   1 
ATOM   1707 C  CA  . PRO   A 1 224 ? 13.223 -18.667 52.475  1.00 48.38  ? 917  PRO   A CA  1 
ATOM   1708 C  C   . PRO   A 1 224 ? 11.983 -19.110 53.236  1.00 49.86  ? 917  PRO   A C   1 
ATOM   1709 O  O   . PRO   A 1 224 ? 11.622 -20.276 53.156  1.00 50.43  ? 917  PRO   A O   1 
ATOM   1710 C  CB  . PRO   A 1 224 ? 12.949 -18.521 50.971  1.00 48.50  ? 917  PRO   A CB  1 
ATOM   1711 C  CG  . PRO   A 1 224 ? 13.384 -19.776 50.380  1.00 48.53  ? 917  PRO   A CG  1 
ATOM   1712 C  CD  . PRO   A 1 224 ? 14.517 -20.309 51.220  1.00 47.08  ? 917  PRO   A CD  1 
ATOM   1713 N  N   . TYR   A 1 225 ? 11.367 -18.198 54.016  1.00 50.41  ? 918  TYR   A N   1 
ATOM   1714 C  CA  . TYR   A 1 225 ? 10.174 -18.449 54.834  1.00 51.23  ? 918  TYR   A CA  1 
ATOM   1715 C  C   . TYR   A 1 225 ? 10.414 -19.644 55.747  1.00 52.39  ? 918  TYR   A C   1 
ATOM   1716 O  O   . TYR   A 1 225 ? 9.620  -20.585 55.774  1.00 52.12  ? 918  TYR   A O   1 
ATOM   1717 C  CB  . TYR   A 1 225 ? 8.913  -18.648 53.968  1.00 51.39  ? 918  TYR   A CB  1 
ATOM   1718 C  CG  . TYR   A 1 225 ? 8.794  -17.690 52.801  1.00 52.72  ? 918  TYR   A CG  1 
ATOM   1719 C  CD1 . TYR   A 1 225 ? 8.327  -16.396 52.982  1.00 53.86  ? 918  TYR   A CD1 1 
ATOM   1720 C  CD2 . TYR   A 1 225 ? 9.115  -18.090 51.511  1.00 53.55  ? 918  TYR   A CD2 1 
ATOM   1721 C  CE1 . TYR   A 1 225 ? 8.213  -15.515 51.914  1.00 54.64  ? 918  TYR   A CE1 1 
ATOM   1722 C  CE2 . TYR   A 1 225 ? 9.010  -17.216 50.439  1.00 54.44  ? 918  TYR   A CE2 1 
ATOM   1723 C  CZ  . TYR   A 1 225 ? 8.557  -15.928 50.644  1.00 55.59  ? 918  TYR   A CZ  1 
ATOM   1724 O  OH  . TYR   A 1 225 ? 8.448  -15.055 49.586  1.00 57.77  ? 918  TYR   A OH  1 
ATOM   1725 N  N   . ASP   A 1 226 ? 11.567 -19.644 56.418  1.00 53.60  ? 919  ASP   A N   1 
ATOM   1726 C  CA  . ASP   A 1 226 ? 11.953 -20.763 57.266  1.00 55.59  ? 919  ASP   A CA  1 
ATOM   1727 C  C   . ASP   A 1 226 ? 10.983 -20.957 58.414  1.00 56.92  ? 919  ASP   A C   1 
ATOM   1728 O  O   . ASP   A 1 226 ? 10.738 -20.028 59.182  1.00 57.02  ? 919  ASP   A O   1 
ATOM   1729 C  CB  . ASP   A 1 226 ? 13.379 -20.576 57.804  1.00 58.05  ? 919  ASP   A CB  1 
ATOM   1730 C  CG  . ASP   A 1 226 ? 13.970 -21.856 58.355  1.00 63.10  ? 919  ASP   A CG  1 
ATOM   1731 O  OD1 . ASP   A 1 226 ? 13.590 -22.943 57.861  1.00 63.97  ? 919  ASP   A OD1 1 
ATOM   1732 O  OD2 . ASP   A 1 226 ? 14.819 -21.771 59.280  1.00 65.12  ? 919  ASP   A OD2 1 
ATOM   1733 N  N   . GLY   A 1 227 ? 10.417 -22.152 58.503  1.00 57.72  ? 920  GLY   A N   1 
ATOM   1734 C  CA  . GLY   A 1 227 ? 9.469  -22.471 59.563  1.00 58.93  ? 920  GLY   A CA  1 
ATOM   1735 C  C   . GLY   A 1 227 ? 8.010  -22.344 59.160  1.00 59.49  ? 920  GLY   A C   1 
ATOM   1736 O  O   . GLY   A 1 227 ? 7.146  -23.020 59.733  1.00 60.10  ? 920  GLY   A O   1 
ATOM   1737 N  N   . ILE   A 1 228 ? 7.714  -21.462 58.187  1.00 58.54  ? 921  ILE   A N   1 
ATOM   1738 C  CA  . ILE   A 1 228 ? 6.351  -21.265 57.705  1.00 57.97  ? 921  ILE   A CA  1 
ATOM   1739 C  C   . ILE   A 1 228 ? 5.989  -22.416 56.783  1.00 57.72  ? 921  ILE   A C   1 
ATOM   1740 O  O   . ILE   A 1 228 ? 6.777  -22.765 55.911  1.00 57.80  ? 921  ILE   A O   1 
ATOM   1741 C  CB  . ILE   A 1 228 ? 6.243  -19.920 56.974  1.00 58.18  ? 921  ILE   A CB  1 
ATOM   1742 C  CG1 . ILE   A 1 228 ? 6.687  -18.764 57.890  1.00 58.68  ? 921  ILE   A CG1 1 
ATOM   1743 C  CG2 . ILE   A 1 228 ? 4.842  -19.714 56.410  1.00 58.56  ? 921  ILE   A CG2 1 
ATOM   1744 C  CD1 . ILE   A 1 228 ? 6.747  -17.398 57.228  1.00 59.48  ? 921  ILE   A CD1 1 
ATOM   1745 N  N   . PRO   A 1 229 ? 4.831  -23.066 56.991  1.00 57.31  ? 922  PRO   A N   1 
ATOM   1746 C  CA  . PRO   A 1 229 ? 4.467  -24.203 56.125  1.00 56.41  ? 922  PRO   A CA  1 
ATOM   1747 C  C   . PRO   A 1 229 ? 4.143  -23.750 54.714  1.00 55.26  ? 922  PRO   A C   1 
ATOM   1748 O  O   . PRO   A 1 229 ? 3.561  -22.688 54.540  1.00 54.97  ? 922  PRO   A O   1 
ATOM   1749 C  CB  . PRO   A 1 229 ? 3.229  -24.807 56.807  1.00 57.01  ? 922  PRO   A CB  1 
ATOM   1750 C  CG  . PRO   A 1 229 ? 3.145  -24.144 58.144  1.00 57.82  ? 922  PRO   A CG  1 
ATOM   1751 C  CD  . PRO   A 1 229 ? 3.807  -22.817 58.022  1.00 56.67  ? 922  PRO   A CD  1 
ATOM   1752 N  N   . ALA   A 1 230 ? 4.487  -24.566 53.717  1.00 54.52  ? 923  ALA   A N   1 
ATOM   1753 C  CA  . ALA   A 1 230 ? 4.230  -24.250 52.316  1.00 54.26  ? 923  ALA   A CA  1 
ATOM   1754 C  C   . ALA   A 1 230 ? 2.746  -23.983 52.038  1.00 54.12  ? 923  ALA   A C   1 
ATOM   1755 O  O   . ALA   A 1 230 ? 2.413  -23.131 51.213  1.00 54.45  ? 923  ALA   A O   1 
ATOM   1756 C  CB  . ALA   A 1 230 ? 4.747  -25.368 51.422  1.00 54.04  ? 923  ALA   A CB  1 
ATOM   1757 N  N   . SER   A 1 231 ? 1.864  -24.674 52.754  1.00 53.62  ? 924  SER   A N   1 
ATOM   1758 C  CA  . SER   A 1 231 ? 0.423  -24.506 52.615  1.00 54.12  ? 924  SER   A CA  1 
ATOM   1759 C  C   . SER   A 1 231 ? -0.052 -23.090 52.952  1.00 54.60  ? 924  SER   A C   1 
ATOM   1760 O  O   . SER   A 1 231 ? -1.135 -22.693 52.521  1.00 54.91  ? 924  SER   A O   1 
ATOM   1761 C  CB  . SER   A 1 231 ? -0.300 -25.497 53.517  1.00 55.64  ? 924  SER   A CB  1 
ATOM   1762 O  OG  . SER   A 1 231 ? 0.105  -25.320 54.865  1.00 57.61  ? 924  SER   A OG  1 
ATOM   1763 N  N   . GLU   A 1 232 ? 0.748  -22.326 53.718  1.00 54.45  ? 925  GLU   A N   1 
ATOM   1764 C  CA  . GLU   A 1 232 ? 0.406  -20.969 54.132  1.00 54.61  ? 925  GLU   A CA  1 
ATOM   1765 C  C   . GLU   A 1 232 ? 1.078  -19.863 53.315  1.00 53.71  ? 925  GLU   A C   1 
ATOM   1766 O  O   . GLU   A 1 232 ? 0.766  -18.697 53.545  1.00 54.03  ? 925  GLU   A O   1 
ATOM   1767 C  CB  . GLU   A 1 232 ? 0.786  -20.758 55.604  1.00 57.95  ? 925  GLU   A CB  1 
ATOM   1768 C  CG  . GLU   A 1 232 ? 0.222  -21.801 56.551  1.00 64.26  ? 925  GLU   A CG  1 
ATOM   1769 C  CD  . GLU   A 1 232 ? 0.582  -21.591 58.008  1.00 73.57  ? 925  GLU   A CD  1 
ATOM   1770 O  OE1 . GLU   A 1 232 ? 1.198  -20.550 58.338  1.00 74.84  ? 925  GLU   A OE1 1 
ATOM   1771 O  OE2 . GLU   A 1 232 ? 0.256  -22.483 58.824  1.00 77.85  ? 925  GLU   A OE2 1 
ATOM   1772 N  N   . ILE   A 1 233 ? 2.011  -20.200 52.403  1.00 52.37  ? 926  ILE   A N   1 
ATOM   1773 C  CA  . ILE   A 1 233 ? 2.768  -19.190 51.653  1.00 51.45  ? 926  ILE   A CA  1 
ATOM   1774 C  C   . ILE   A 1 233 ? 1.873  -18.256 50.825  1.00 51.14  ? 926  ILE   A C   1 
ATOM   1775 O  O   . ILE   A 1 233 ? 1.981  -17.045 51.006  1.00 51.24  ? 926  ILE   A O   1 
ATOM   1776 C  CB  . ILE   A 1 233 ? 3.917  -19.817 50.812  1.00 50.95  ? 926  ILE   A CB  1 
ATOM   1777 C  CG1 . ILE   A 1 233 ? 4.971  -20.446 51.736  1.00 51.05  ? 926  ILE   A CG1 1 
ATOM   1778 C  CG2 . ILE   A 1 233 ? 4.569  -18.798 49.869  1.00 51.01  ? 926  ILE   A CG2 1 
ATOM   1779 C  CD1 . ILE   A 1 233 ? 5.609  -19.490 52.698  1.00 51.47  ? 926  ILE   A CD1 1 
ATOM   1780 N  N   . SER   A 1 234 ? 0.950  -18.780 49.999  1.00 50.53  ? 927  SER   A N   1 
ATOM   1781 C  CA  . SER   A 1 234 ? 0.073  -17.922 49.200  1.00 50.66  ? 927  SER   A CA  1 
ATOM   1782 C  C   . SER   A 1 234 ? -0.691 -16.894 50.031  1.00 50.84  ? 927  SER   A C   1 
ATOM   1783 O  O   . SER   A 1 234 ? -0.837 -15.753 49.609  1.00 51.08  ? 927  SER   A O   1 
ATOM   1784 C  CB  . SER   A 1 234 ? -0.897 -18.759 48.378  1.00 52.20  ? 927  SER   A CB  1 
ATOM   1785 O  OG  . SER   A 1 234 ? -1.879 -19.363 49.204  1.00 54.74  ? 927  SER   A OG  1 
ATOM   1786 N  N   . SER   A 1 235 ? -1.132 -17.286 51.235  1.00 50.63  ? 928  SER   A N   1 
ATOM   1787 C  CA  . SER   A 1 235 ? -1.841 -16.394 52.149  1.00 50.56  ? 928  SER   A CA  1 
ATOM   1788 C  C   . SER   A 1 235 ? -0.910 -15.329 52.730  1.00 49.60  ? 928  SER   A C   1 
ATOM   1789 O  O   . SER   A 1 235 ? -1.330 -14.196 52.937  1.00 49.88  ? 928  SER   A O   1 
ATOM   1790 C  CB  . SER   A 1 235 ? -2.478 -17.186 53.278  1.00 52.73  ? 928  SER   A CB  1 
ATOM   1791 O  OG  . SER   A 1 235 ? -3.238 -16.315 54.101  1.00 56.37  ? 928  SER   A OG  1 
ATOM   1792 N  N   . ILE   A 1 236 ? 0.347  -15.694 52.997  1.00 48.53  ? 929  ILE   A N   1 
ATOM   1793 C  CA  . ILE   A 1 236 ? 1.381  -14.778 53.480  1.00 47.80  ? 929  ILE   A CA  1 
ATOM   1794 C  C   . ILE   A 1 236 ? 1.634  -13.715 52.395  1.00 46.45  ? 929  ILE   A C   1 
ATOM   1795 O  O   . ILE   A 1 236 ? 1.667  -12.522 52.695  1.00 45.95  ? 929  ILE   A O   1 
ATOM   1796 C  CB  . ILE   A 1 236 ? 2.671  -15.581 53.899  1.00 48.42  ? 929  ILE   A CB  1 
ATOM   1797 C  CG1 . ILE   A 1 236 ? 2.825  -15.622 55.415  1.00 49.83  ? 929  ILE   A CG1 1 
ATOM   1798 C  CG2 . ILE   A 1 236 ? 3.980  -15.141 53.227  1.00 48.42  ? 929  ILE   A CG2 1 
ATOM   1799 C  CD1 . ILE   A 1 236 ? 2.518  -16.975 55.980  1.00 51.55  ? 929  ILE   A CD1 1 
ATOM   1800 N  N   . LEU   A 1 237 ? 1.742  -14.161 51.126  1.00 45.52  ? 930  LEU   A N   1 
ATOM   1801 C  CA  . LEU   A 1 237 ? 1.986  -13.292 49.987  1.00 44.97  ? 930  LEU   A CA  1 
ATOM   1802 C  C   . LEU   A 1 237 ? 0.829  -12.332 49.775  1.00 45.03  ? 930  LEU   A C   1 
ATOM   1803 O  O   . LEU   A 1 237 ? 1.064  -11.162 49.474  1.00 45.24  ? 930  LEU   A O   1 
ATOM   1804 C  CB  . LEU   A 1 237 ? 2.230  -14.119 48.712  1.00 44.55  ? 930  LEU   A CB  1 
ATOM   1805 C  CG  . LEU   A 1 237 ? 3.385  -15.120 48.740  1.00 44.88  ? 930  LEU   A CG  1 
ATOM   1806 C  CD1 . LEU   A 1 237 ? 3.487  -15.866 47.422  1.00 44.80  ? 930  LEU   A CD1 1 
ATOM   1807 C  CD2 . LEU   A 1 237 ? 4.697  -14.449 49.094  1.00 45.23  ? 930  LEU   A CD2 1 
ATOM   1808 N  N   . GLU   A 1 238 ? -0.416 -12.815 49.952  1.00 44.61  ? 931  GLU   A N   1 
ATOM   1809 C  CA  . GLU   A 1 238 ? -1.621 -11.997 49.800  1.00 44.65  ? 931  GLU   A CA  1 
ATOM   1810 C  C   . GLU   A 1 238 ? -1.716 -10.919 50.872  1.00 44.97  ? 931  GLU   A C   1 
ATOM   1811 O  O   . GLU   A 1 238 ? -2.151 -9.801  50.588  1.00 45.44  ? 931  GLU   A O   1 
ATOM   1812 C  CB  . GLU   A 1 238 ? -2.872 -12.873 49.762  1.00 46.49  ? 931  GLU   A CB  1 
ATOM   1813 C  CG  . GLU   A 1 238 ? -3.100 -13.475 48.391  1.00 51.12  ? 931  GLU   A CG  1 
ATOM   1814 C  CD  . GLU   A 1 238 ? -3.951 -14.727 48.369  1.00 58.54  ? 931  GLU   A CD  1 
ATOM   1815 O  OE1 . GLU   A 1 238 ? -4.816 -14.842 47.473  1.00 60.75  ? 931  GLU   A OE1 1 
ATOM   1816 O  OE2 . GLU   A 1 238 ? -3.747 -15.601 49.241  1.00 60.83  ? 931  GLU   A OE2 1 
ATOM   1817 N  N   . LYS   A 1 239 ? -1.247 -11.222 52.089  1.00 44.53  ? 932  LYS   A N   1 
ATOM   1818 C  CA  . LYS   A 1 239 ? -1.223 -10.239 53.178  1.00 44.45  ? 932  LYS   A CA  1 
ATOM   1819 C  C   . LYS   A 1 239 ? -0.160 -9.142  52.983  1.00 43.80  ? 932  LYS   A C   1 
ATOM   1820 O  O   . LYS   A 1 239 ? -0.164 -8.155  53.719  1.00 44.09  ? 932  LYS   A O   1 
ATOM   1821 C  CB  . LYS   A 1 239 ? -1.020 -10.926 54.546  1.00 46.73  ? 932  LYS   A CB  1 
ATOM   1822 C  CG  . LYS   A 1 239 ? -2.242 -11.672 55.058  1.00 51.43  ? 932  LYS   A CG  1 
ATOM   1823 C  CD  . LYS   A 1 239 ? -2.054 -12.126 56.509  1.00 57.82  ? 932  LYS   A CD  1 
ATOM   1824 C  CE  . LYS   A 1 239 ? -1.020 -13.225 56.668  1.00 63.01  ? 932  LYS   A CE  1 
ATOM   1825 N  NZ  . LYS   A 1 239 ? -1.030 -13.821 58.039  1.00 65.42  ? 932  LYS   A NZ  1 
ATOM   1826 N  N   . GLY   A 1 240 ? 0.751  -9.333  52.034  1.00 42.89  ? 933  GLY   A N   1 
ATOM   1827 C  CA  . GLY   A 1 240 ? 1.826  -8.391  51.761  1.00 42.57  ? 933  GLY   A CA  1 
ATOM   1828 C  C   . GLY   A 1 240 ? 3.154  -8.730  52.406  1.00 41.88  ? 933  GLY   A C   1 
ATOM   1829 O  O   . GLY   A 1 240 ? 4.069  -7.909  52.410  1.00 41.90  ? 933  GLY   A O   1 
ATOM   1830 N  N   . GLU   A 1 241 ? 3.276  -9.940  52.947  1.00 41.39  ? 934  GLU   A N   1 
ATOM   1831 C  CA  . GLU   A 1 241 ? 4.511  -10.379 53.579  1.00 41.61  ? 934  GLU   A CA  1 
ATOM   1832 C  C   . GLU   A 1 241 ? 5.508  -10.837 52.522  1.00 40.29  ? 934  GLU   A C   1 
ATOM   1833 O  O   . GLU   A 1 241 ? 5.152  -11.550 51.585  1.00 40.67  ? 934  GLU   A O   1 
ATOM   1834 C  CB  . GLU   A 1 241 ? 4.239  -11.515 54.577  1.00 45.76  ? 934  GLU   A CB  1 
ATOM   1835 C  CG  . GLU   A 1 241 ? 3.353  -11.113 55.745  1.00 54.14  ? 934  GLU   A CG  1 
ATOM   1836 C  CD  . GLU   A 1 241 ? 3.314  -12.160 56.846  1.00 66.91  ? 934  GLU   A CD  1 
ATOM   1837 O  OE1 . GLU   A 1 241 ? 4.384  -12.731 57.168  1.00 70.24  ? 934  GLU   A OE1 1 
ATOM   1838 O  OE2 . GLU   A 1 241 ? 2.210  -12.412 57.388  1.00 70.13  ? 934  GLU   A OE2 1 
ATOM   1839 N  N   . ARG   A 1 242 ? 6.745  -10.401 52.654  1.00 38.47  ? 935  ARG   A N   1 
ATOM   1840 C  CA  . ARG   A 1 242 ? 7.807  -10.766 51.727  1.00 36.92  ? 935  ARG   A CA  1 
ATOM   1841 C  C   . ARG   A 1 242 ? 9.054  -11.170 52.514  1.00 36.10  ? 935  ARG   A C   1 
ATOM   1842 O  O   . ARG   A 1 242 ? 9.147  -10.918 53.722  1.00 36.34  ? 935  ARG   A O   1 
ATOM   1843 C  CB  . ARG   A 1 242 ? 8.141  -9.591  50.781  1.00 36.89  ? 935  ARG   A CB  1 
ATOM   1844 C  CG  . ARG   A 1 242 ? 7.035  -9.187  49.835  1.00 37.55  ? 935  ARG   A CG  1 
ATOM   1845 C  CD  . ARG   A 1 242 ? 6.655  -10.310 48.904  1.00 38.78  ? 935  ARG   A CD  1 
ATOM   1846 N  NE  . ARG   A 1 242 ? 5.665  -9.895  47.912  1.00 39.22  ? 935  ARG   A NE  1 
ATOM   1847 C  CZ  . ARG   A 1 242 ? 4.352  -9.893  48.115  1.00 39.31  ? 935  ARG   A CZ  1 
ATOM   1848 N  NH1 . ARG   A 1 242 ? 3.530  -9.505  47.155  1.00 39.96  ? 935  ARG   A NH1 1 
ATOM   1849 N  NH2 . ARG   A 1 242 ? 3.853  -10.267 49.283  1.00 37.52  ? 935  ARG   A NH2 1 
ATOM   1850 N  N   . LEU   A 1 243 ? 10.044 -11.753 51.824  1.00 35.22  ? 936  LEU   A N   1 
ATOM   1851 C  CA  . LEU   A 1 243 ? 11.298 -12.144 52.445  1.00 35.00  ? 936  LEU   A CA  1 
ATOM   1852 C  C   . LEU   A 1 243 ? 11.995 -10.928 53.045  1.00 34.83  ? 936  LEU   A C   1 
ATOM   1853 O  O   . LEU   A 1 243 ? 11.979 -9.852  52.445  1.00 35.14  ? 936  LEU   A O   1 
ATOM   1854 C  CB  . LEU   A 1 243 ? 12.196 -12.826 51.398  1.00 35.07  ? 936  LEU   A CB  1 
ATOM   1855 C  CG  . LEU   A 1 243 ? 11.801 -14.243 51.031  1.00 35.53  ? 936  LEU   A CG  1 
ATOM   1856 C  CD1 . LEU   A 1 243 ? 12.673 -14.774 49.915  1.00 35.84  ? 936  LEU   A CD1 1 
ATOM   1857 C  CD2 . LEU   A 1 243 ? 11.885 -15.147 52.233  1.00 35.72  ? 936  LEU   A CD2 1 
ATOM   1858 N  N   . PRO   A 1 244 ? 12.522 -11.054 54.269  1.00 34.60  ? 937  PRO   A N   1 
ATOM   1859 C  CA  . PRO   A 1 244 ? 13.152 -9.890  54.917  1.00 34.79  ? 937  PRO   A CA  1 
ATOM   1860 C  C   . PRO   A 1 244 ? 14.366 -9.333  54.185  1.00 35.39  ? 937  PRO   A C   1 
ATOM   1861 O  O   . PRO   A 1 244 ? 14.974 -10.006 53.371  1.00 35.31  ? 937  PRO   A O   1 
ATOM   1862 C  CB  . PRO   A 1 244 ? 13.533 -10.415 56.302  1.00 35.14  ? 937  PRO   A CB  1 
ATOM   1863 C  CG  . PRO   A 1 244 ? 13.602 -11.902 56.148  1.00 35.18  ? 937  PRO   A CG  1 
ATOM   1864 C  CD  . PRO   A 1 244 ? 12.565 -12.249 55.129  1.00 33.71  ? 937  PRO   A CD  1 
ATOM   1865 N  N   . GLN   A 1 245 ? 14.696 -8.091  54.463  1.00 36.59  ? 938  GLN   A N   1 
ATOM   1866 C  CA  . GLN   A 1 245 ? 15.840 -7.426  53.866  1.00 38.16  ? 938  GLN   A CA  1 
ATOM   1867 C  C   . GLN   A 1 245 ? 17.114 -7.973  54.503  1.00 40.01  ? 938  GLN   A C   1 
ATOM   1868 O  O   . GLN   A 1 245 ? 17.257 -7.923  55.727  1.00 41.06  ? 938  GLN   A O   1 
ATOM   1869 C  CB  . GLN   A 1 245 ? 15.718 -5.916  54.082  1.00 39.13  ? 938  GLN   A CB  1 
ATOM   1870 C  CG  . GLN   A 1 245 ? 16.933 -5.128  53.626  1.00 42.19  ? 938  GLN   A CG  1 
ATOM   1871 C  CD  . GLN   A 1 245 ? 16.835 -3.630  53.847  1.00 45.56  ? 938  GLN   A CD  1 
ATOM   1872 O  OE1 . GLN   A 1 245 ? 17.790 -2.891  53.584  1.00 46.55  ? 938  GLN   A OE1 1 
ATOM   1873 N  NE2 . GLN   A 1 245 ? 15.693 -3.128  54.325  1.00 45.93  ? 938  GLN   A NE2 1 
ATOM   1874 N  N   . PRO   A 1 246 ? 18.035 -8.545  53.705  1.00 40.22  ? 939  PRO   A N   1 
ATOM   1875 C  CA  . PRO   A 1 246 ? 19.257 -9.113  54.295  1.00 40.24  ? 939  PRO   A CA  1 
ATOM   1876 C  C   . PRO   A 1 246 ? 20.130 -8.045  54.942  1.00 40.44  ? 939  PRO   A C   1 
ATOM   1877 O  O   . PRO   A 1 246 ? 20.177 -6.912  54.467  1.00 40.89  ? 939  PRO   A O   1 
ATOM   1878 C  CB  . PRO   A 1 246 ? 19.942 -9.794  53.105  1.00 40.63  ? 939  PRO   A CB  1 
ATOM   1879 C  CG  . PRO   A 1 246 ? 18.860 -9.952  52.073  1.00 41.05  ? 939  PRO   A CG  1 
ATOM   1880 C  CD  . PRO   A 1 246 ? 18.002 -8.745  52.247  1.00 39.65  ? 939  PRO   A CD  1 
ATOM   1881 N  N   . PRO   A 1 247 ? 20.792 -8.380  56.062  1.00 40.19  ? 940  PRO   A N   1 
ATOM   1882 C  CA  . PRO   A 1 247 ? 21.604 -7.383  56.770  1.00 40.31  ? 940  PRO   A CA  1 
ATOM   1883 C  C   . PRO   A 1 247 ? 22.664 -6.674  55.936  1.00 41.17  ? 940  PRO   A C   1 
ATOM   1884 O  O   . PRO   A 1 247 ? 22.917 -5.503  56.189  1.00 41.98  ? 940  PRO   A O   1 
ATOM   1885 C  CB  . PRO   A 1 247 ? 22.216 -8.188  57.915  1.00 40.62  ? 940  PRO   A CB  1 
ATOM   1886 C  CG  . PRO   A 1 247 ? 21.223 -9.258  58.168  1.00 40.86  ? 940  PRO   A CG  1 
ATOM   1887 C  CD  . PRO   A 1 247 ? 20.756 -9.653  56.803  1.00 39.63  ? 940  PRO   A CD  1 
ATOM   1888 N  N   . ILE   A 1 248 ? 23.261 -7.342  54.938  1.00 41.12  ? 941  ILE   A N   1 
ATOM   1889 C  CA  . ILE   A 1 248 ? 24.268 -6.688  54.095  1.00 41.62  ? 941  ILE   A CA  1 
ATOM   1890 C  C   . ILE   A 1 248 ? 23.683 -5.735  53.052  1.00 42.37  ? 941  ILE   A C   1 
ATOM   1891 O  O   . ILE   A 1 248 ? 24.407 -4.886  52.537  1.00 42.36  ? 941  ILE   A O   1 
ATOM   1892 C  CB  . ILE   A 1 248 ? 25.198 -7.710  53.418  1.00 41.76  ? 941  ILE   A CB  1 
ATOM   1893 C  CG1 . ILE   A 1 248 ? 24.448 -8.536  52.357  1.00 42.09  ? 941  ILE   A CG1 1 
ATOM   1894 C  CG2 . ILE   A 1 248 ? 25.884 -8.580  54.466  1.00 42.39  ? 941  ILE   A CG2 1 
ATOM   1895 C  CD1 . ILE   A 1 248 ? 25.323 -9.439  51.556  1.00 43.29  ? 941  ILE   A CD1 1 
ATOM   1896 N  N   . CYS   A 1 249 ? 22.393 -5.873  52.723  1.00 42.60  ? 942  CYS   A N   1 
ATOM   1897 C  CA  . CYS   A 1 249 ? 21.785 -5.078  51.662  1.00 43.02  ? 942  CYS   A CA  1 
ATOM   1898 C  C   . CYS   A 1 249 ? 21.406 -3.682  52.016  1.00 43.98  ? 942  CYS   A C   1 
ATOM   1899 O  O   . CYS   A 1 249 ? 20.678 -3.448  52.979  1.00 44.61  ? 942  CYS   A O   1 
ATOM   1900 C  CB  . CYS   A 1 249 ? 20.584 -5.802  51.081  1.00 42.95  ? 942  CYS   A CB  1 
ATOM   1901 S  SG  . CYS   A 1 249 ? 20.990 -7.402  50.380  1.00 44.10  ? 942  CYS   A SG  1 
ATOM   1902 N  N   . THR   A 1 250 ? 21.774 -2.759  51.128  1.00 44.05  ? 943  THR   A N   1 
ATOM   1903 C  CA  . THR   A 1 250 ? 21.291 -1.393  51.198  1.00 44.38  ? 943  THR   A CA  1 
ATOM   1904 C  C   . THR   A 1 250 ? 19.849 -1.428  50.644  1.00 44.65  ? 943  THR   A C   1 
ATOM   1905 O  O   . THR   A 1 250 ? 19.433 -2.438  50.055  1.00 45.09  ? 943  THR   A O   1 
ATOM   1906 C  CB  . THR   A 1 250 ? 22.187 -0.473  50.378  1.00 45.43  ? 943  THR   A CB  1 
ATOM   1907 O  OG1 . THR   A 1 250 ? 22.240 -0.955  49.038  1.00 46.80  ? 943  THR   A OG1 1 
ATOM   1908 C  CG2 . THR   A 1 250 ? 23.581 -0.343  50.974  1.00 45.55  ? 943  THR   A CG2 1 
ATOM   1909 N  N   . ILE   A 1 251 ? 19.078 -0.349  50.833  1.00 44.33  ? 944  ILE   A N   1 
ATOM   1910 C  CA  . ILE   A 1 251 ? 17.698 -0.340  50.337  1.00 43.78  ? 944  ILE   A CA  1 
ATOM   1911 C  C   . ILE   A 1 251 ? 17.650 -0.379  48.788  1.00 43.37  ? 944  ILE   A C   1 
ATOM   1912 O  O   . ILE   A 1 251 ? 16.687 -0.909  48.243  1.00 43.48  ? 944  ILE   A O   1 
ATOM   1913 C  CB  . ILE   A 1 251 ? 16.855 0.790   50.959  1.00 43.30  ? 944  ILE   A CB  1 
ATOM   1914 C  CG1 . ILE   A 1 251 ? 15.357 0.509   50.807  1.00 43.59  ? 944  ILE   A CG1 1 
ATOM   1915 C  CG2 . ILE   A 1 251 ? 17.244 2.119   50.392  1.00 43.57  ? 944  ILE   A CG2 1 
ATOM   1916 C  CD1 . ILE   A 1 251 ? 14.905 -0.751  51.459  1.00 44.64  ? 944  ILE   A CD1 1 
ATOM   1917 N  N   . ASP   A 1 252 ? 18.720 0.070   48.097  1.00 42.93  ? 945  ASP   A N   1 
ATOM   1918 C  CA  . ASP   A 1 252 ? 18.798 0.050   46.633  1.00 43.66  ? 945  ASP   A CA  1 
ATOM   1919 C  C   . ASP   A 1 252 ? 18.755 -1.375  46.094  1.00 43.03  ? 945  ASP   A C   1 
ATOM   1920 O  O   . ASP   A 1 252 ? 18.068 -1.648  45.111  1.00 42.98  ? 945  ASP   A O   1 
ATOM   1921 C  CB  . ASP   A 1 252 ? 20.096 0.715   46.147  1.00 46.86  ? 945  ASP   A CB  1 
ATOM   1922 C  CG  . ASP   A 1 252 ? 20.334 2.122   46.660  1.00 53.18  ? 945  ASP   A CG  1 
ATOM   1923 O  OD1 . ASP   A 1 252 ? 20.433 2.298   47.904  1.00 54.06  ? 945  ASP   A OD1 1 
ATOM   1924 O  OD2 . ASP   A 1 252 ? 20.462 3.040   45.822  1.00 55.95  ? 945  ASP   A OD2 1 
ATOM   1925 N  N   . VAL   A 1 253 ? 19.502 -2.279  46.747  1.00 42.40  ? 946  VAL   A N   1 
ATOM   1926 C  CA  . VAL   A 1 253 ? 19.585 -3.692  46.392  1.00 41.66  ? 946  VAL   A CA  1 
ATOM   1927 C  C   . VAL   A 1 253 ? 18.301 -4.395  46.775  1.00 40.66  ? 946  VAL   A C   1 
ATOM   1928 O  O   . VAL   A 1 253 ? 17.773 -5.164  45.973  1.00 40.52  ? 946  VAL   A O   1 
ATOM   1929 C  CB  . VAL   A 1 253 ? 20.823 -4.354  47.050  1.00 41.96  ? 946  VAL   A CB  1 
ATOM   1930 C  CG1 . VAL   A 1 253 ? 20.937 -5.826  46.668  1.00 41.97  ? 946  VAL   A CG1 1 
ATOM   1931 C  CG2 . VAL   A 1 253 ? 22.088 -3.605  46.664  1.00 42.34  ? 946  VAL   A CG2 1 
ATOM   1932 N  N   . TYR   A 1 254 ? 17.773 -4.107  47.979  1.00 40.09  ? 947  TYR   A N   1 
ATOM   1933 C  CA  . TYR   A 1 254 ? 16.543 -4.739  48.443  1.00 40.67  ? 947  TYR   A CA  1 
ATOM   1934 C  C   . TYR   A 1 254 ? 15.328 -4.376  47.598  1.00 41.05  ? 947  TYR   A C   1 
ATOM   1935 O  O   . TYR   A 1 254 ? 14.476 -5.228  47.365  1.00 41.39  ? 947  TYR   A O   1 
ATOM   1936 C  CB  . TYR   A 1 254 ? 16.281 -4.488  49.928  1.00 41.00  ? 947  TYR   A CB  1 
ATOM   1937 C  CG  . TYR   A 1 254 ? 15.053 -5.225  50.420  1.00 42.58  ? 947  TYR   A CG  1 
ATOM   1938 C  CD1 . TYR   A 1 254 ? 15.010 -6.613  50.434  1.00 43.42  ? 947  TYR   A CD1 1 
ATOM   1939 C  CD2 . TYR   A 1 254 ? 13.913 -4.537  50.808  1.00 43.78  ? 947  TYR   A CD2 1 
ATOM   1940 C  CE1 . TYR   A 1 254 ? 13.876 -7.295  50.853  1.00 44.25  ? 947  TYR   A CE1 1 
ATOM   1941 C  CE2 . TYR   A 1 254 ? 12.775 -5.209  51.228  1.00 44.69  ? 947  TYR   A CE2 1 
ATOM   1942 C  CZ  . TYR   A 1 254 ? 12.766 -6.588  51.265  1.00 45.44  ? 947  TYR   A CZ  1 
ATOM   1943 O  OH  . TYR   A 1 254 ? 11.648 -7.256  51.691  1.00 47.21  ? 947  TYR   A OH  1 
ATOM   1944 N  N   . MET   A 1 255 ? 15.258 -3.140  47.113  1.00 41.07  ? 948  MET   A N   1 
ATOM   1945 C  CA  . MET   A 1 255 ? 14.144 -2.720  46.278  1.00 41.52  ? 948  MET   A CA  1 
ATOM   1946 C  C   . MET   A 1 255 ? 14.087 -3.519  44.973  1.00 41.90  ? 948  MET   A C   1 
ATOM   1947 O  O   . MET   A 1 255 ? 12.991 -3.798  44.506  1.00 42.31  ? 948  MET   A O   1 
ATOM   1948 C  CB  . MET   A 1 255 ? 14.145 -1.205  46.065  1.00 42.21  ? 948  MET   A CB  1 
ATOM   1949 C  CG  . MET   A 1 255 ? 13.704 -0.439  47.297  1.00 44.15  ? 948  MET   A CG  1 
ATOM   1950 S  SD  . MET   A 1 255 ? 11.981 -0.782  47.720  1.00 48.97  ? 948  MET   A SD  1 
ATOM   1951 C  CE  . MET   A 1 255 ? 12.177 -1.721  49.197  1.00 47.12  ? 948  MET   A CE  1 
ATOM   1952 N  N   . ILE   A 1 256 ? 15.246 -3.967  44.436  1.00 41.27  ? 949  ILE   A N   1 
ATOM   1953 C  CA  . ILE   A 1 256 ? 15.273 -4.790  43.229  1.00 40.87  ? 949  ILE   A CA  1 
ATOM   1954 C  C   . ILE   A 1 256 ? 14.608 -6.136  43.505  1.00 40.77  ? 949  ILE   A C   1 
ATOM   1955 O  O   . ILE   A 1 256 ? 13.768 -6.572  42.713  1.00 40.68  ? 949  ILE   A O   1 
ATOM   1956 C  CB  . ILE   A 1 256 ? 16.696 -4.978  42.654  1.00 41.19  ? 949  ILE   A CB  1 
ATOM   1957 C  CG1 . ILE   A 1 256 ? 17.361 -3.645  42.298  1.00 42.07  ? 949  ILE   A CG1 1 
ATOM   1958 C  CG2 . ILE   A 1 256 ? 16.641 -5.884  41.443  1.00 41.78  ? 949  ILE   A CG2 1 
ATOM   1959 C  CD1 . ILE   A 1 256 ? 18.774 -3.749  41.697  1.00 43.02  ? 949  ILE   A CD1 1 
ATOM   1960 N  N   . MET   A 1 257 ? 14.973 -6.796  44.637  1.00 40.57  ? 950  MET   A N   1 
ATOM   1961 C  CA  . MET   A 1 257 ? 14.383 -8.079  45.059  1.00 39.98  ? 950  MET   A CA  1 
ATOM   1962 C  C   . MET   A 1 257 ? 12.888 -7.893  45.289  1.00 38.55  ? 950  MET   A C   1 
ATOM   1963 O  O   . MET   A 1 257 ? 12.098 -8.612  44.698  1.00 38.08  ? 950  MET   A O   1 
ATOM   1964 C  CB  . MET   A 1 257 ? 15.012 -8.590  46.367  1.00 41.28  ? 950  MET   A CB  1 
ATOM   1965 C  CG  . MET   A 1 257 ? 16.494 -8.784  46.314  1.00 45.35  ? 950  MET   A CG  1 
ATOM   1966 S  SD  . MET   A 1 257 ? 17.123 -9.316  47.942  1.00 53.63  ? 950  MET   A SD  1 
ATOM   1967 C  CE  . MET   A 1 257 ? 18.522 -8.284  48.039  1.00 51.49  ? 950  MET   A CE  1 
ATOM   1968 N  N   . ARG   A 1 258 ? 12.502 -6.880  46.088  1.00 37.78  ? 951  ARG   A N   1 
ATOM   1969 C  CA  . ARG   A 1 258 ? 11.126 -6.553  46.426  1.00 37.94  ? 951  ARG   A CA  1 
ATOM   1970 C  C   . ARG   A 1 258 ? 10.276 -6.377  45.165  1.00 38.49  ? 951  ARG   A C   1 
ATOM   1971 O  O   . ARG   A 1 258 ? 9.145  -6.849  45.122  1.00 39.19  ? 951  ARG   A O   1 
ATOM   1972 C  CB  . ARG   A 1 258 ? 11.109 -5.303  47.329  1.00 38.70  ? 951  ARG   A CB  1 
ATOM   1973 C  CG  . ARG   A 1 258 ? 9.766  -4.860  47.902  1.00 40.55  ? 951  ARG   A CG  1 
ATOM   1974 C  CD  . ARG   A 1 258 ? 8.963  -5.948  48.590  1.00 42.24  ? 951  ARG   A CD  1 
ATOM   1975 N  NE  . ARG   A 1 258 ? 7.957  -6.456  47.665  1.00 44.67  ? 951  ARG   A NE  1 
ATOM   1976 C  CZ  . ARG   A 1 258 ? 6.655  -6.218  47.747  1.00 46.22  ? 951  ARG   A CZ  1 
ATOM   1977 N  NH1 . ARG   A 1 258 ? 6.161  -5.539  48.773  1.00 45.63  ? 951  ARG   A NH1 1 
ATOM   1978 N  NH2 . ARG   A 1 258 ? 5.832  -6.696  46.829  1.00 46.12  ? 951  ARG   A NH2 1 
ATOM   1979 N  N   . LYS   A 1 259 ? 10.844 -5.781  44.113  1.00 38.33  ? 952  LYS   A N   1 
ATOM   1980 C  CA  . LYS   A 1 259 ? 10.155 -5.580  42.833  1.00 38.09  ? 952  LYS   A CA  1 
ATOM   1981 C  C   . LYS   A 1 259 ? 9.954  -6.889  42.061  1.00 38.52  ? 952  LYS   A C   1 
ATOM   1982 O  O   . LYS   A 1 259 ? 8.962  -7.022  41.354  1.00 39.54  ? 952  LYS   A O   1 
ATOM   1983 C  CB  . LYS   A 1 259 ? 10.881 -4.547  41.978  1.00 38.30  ? 952  LYS   A CB  1 
ATOM   1984 C  CG  . LYS   A 1 259 ? 10.821 -3.152  42.539  1.00 40.35  ? 952  LYS   A CG  1 
ATOM   1985 C  CD  . LYS   A 1 259 ? 11.352 -2.166  41.543  1.00 45.24  ? 952  LYS   A CD  1 
ATOM   1986 C  CE  . LYS   A 1 259 ? 11.157 -0.751  41.993  1.00 50.16  ? 952  LYS   A CE  1 
ATOM   1987 N  NZ  . LYS   A 1 259 ? 10.816 0.127   40.834  1.00 53.49  ? 952  LYS   A NZ  1 
ATOM   1988 N  N   . CYS   A 1 260 ? 10.874 -7.855  42.187  1.00 37.71  ? 953  CYS   A N   1 
ATOM   1989 C  CA  . CYS   A 1 260 ? 10.699 -9.173  41.560  1.00 37.38  ? 953  CYS   A CA  1 
ATOM   1990 C  C   . CYS   A 1 260 ? 9.484  -9.904  42.176  1.00 37.30  ? 953  CYS   A C   1 
ATOM   1991 O  O   . CYS   A 1 260 ? 8.907  -10.773 41.543  1.00 37.38  ? 953  CYS   A O   1 
ATOM   1992 C  CB  . CYS   A 1 260 ? 11.961 -10.018 41.721  1.00 38.12  ? 953  CYS   A CB  1 
ATOM   1993 S  SG  . CYS   A 1 260 ? 13.453 -9.307  40.982  1.00 41.34  ? 953  CYS   A SG  1 
ATOM   1994 N  N   . TRP   A 1 261 ? 9.130  -9.574  43.424  1.00 37.21  ? 954  TRP   A N   1 
ATOM   1995 C  CA  . TRP   A 1 261 ? 8.055  -10.182 44.169  1.00 37.59  ? 954  TRP   A CA  1 
ATOM   1996 C  C   . TRP   A 1 261 ? 6.779  -9.355  44.090  1.00 38.20  ? 954  TRP   A C   1 
ATOM   1997 O  O   . TRP   A 1 261 ? 6.034  -9.289  45.068  1.00 39.45  ? 954  TRP   A O   1 
ATOM   1998 C  CB  . TRP   A 1 261 ? 8.486  -10.383 45.639  1.00 37.30  ? 954  TRP   A CB  1 
ATOM   1999 C  CG  . TRP   A 1 261 ? 9.803  -11.085 45.798  1.00 37.28  ? 954  TRP   A CG  1 
ATOM   2000 C  CD1 . TRP   A 1 261 ? 10.304 -12.084 45.012  1.00 37.92  ? 954  TRP   A CD1 1 
ATOM   2001 C  CD2 . TRP   A 1 261 ? 10.776 -10.851 46.821  1.00 37.07  ? 954  TRP   A CD2 1 
ATOM   2002 N  NE1 . TRP   A 1 261 ? 11.541 -12.464 45.467  1.00 38.03  ? 954  TRP   A NE1 1 
ATOM   2003 C  CE2 . TRP   A 1 261 ? 11.850 -11.732 46.586  1.00 37.80  ? 954  TRP   A CE2 1 
ATOM   2004 C  CE3 . TRP   A 1 261 ? 10.847 -9.977  47.917  1.00 37.45  ? 954  TRP   A CE3 1 
ATOM   2005 C  CZ2 . TRP   A 1 261 ? 12.975 -11.766 47.410  1.00 38.52  ? 954  TRP   A CZ2 1 
ATOM   2006 C  CZ3 . TRP   A 1 261 ? 11.976 -9.994  48.716  1.00 38.19  ? 954  TRP   A CZ3 1 
ATOM   2007 C  CH2 . TRP   A 1 261 ? 13.029 -10.869 48.454  1.00 38.38  ? 954  TRP   A CH2 1 
ATOM   2008 N  N   . MET   A 1 262 ? 6.509  -8.741  42.945  1.00 37.48  ? 955  MET   A N   1 
ATOM   2009 C  CA  . MET   A 1 262 ? 5.283  -7.962  42.774  1.00 38.05  ? 955  MET   A CA  1 
ATOM   2010 C  C   . MET   A 1 262 ? 4.096  -8.874  42.442  1.00 39.60  ? 955  MET   A C   1 
ATOM   2011 O  O   . MET   A 1 262 ? 4.297  -9.930  41.866  1.00 39.85  ? 955  MET   A O   1 
ATOM   2012 C  CB  . MET   A 1 262 ? 5.461  -6.900  41.679  1.00 37.44  ? 955  MET   A CB  1 
ATOM   2013 C  CG  . MET   A 1 262 ? 6.099  -5.628  42.165  1.00 36.69  ? 955  MET   A CG  1 
ATOM   2014 S  SD  . MET   A 1 262 ? 6.148  -4.422  40.824  1.00 37.65  ? 955  MET   A SD  1 
ATOM   2015 C  CE  . MET   A 1 262 ? 7.400  -3.455  41.364  1.00 42.51  ? 955  MET   A CE  1 
ATOM   2016 N  N   . ILE   A 1 263 ? 2.865  -8.468  42.775  1.00 40.73  ? 956  ILE   A N   1 
ATOM   2017 C  CA  . ILE   A 1 263 ? 1.676  -9.263  42.452  1.00 42.28  ? 956  ILE   A CA  1 
ATOM   2018 C  C   . ILE   A 1 263 ? 1.401  -9.193  40.950  1.00 43.16  ? 956  ILE   A C   1 
ATOM   2019 O  O   . ILE   A 1 263 ? 1.144  -10.231 40.344  1.00 43.85  ? 956  ILE   A O   1 
ATOM   2020 C  CB  . ILE   A 1 263 ? 0.437  -8.884  43.319  1.00 43.12  ? 956  ILE   A CB  1 
ATOM   2021 C  CG1 . ILE   A 1 263 ? 0.710  -9.069  44.830  1.00 44.30  ? 956  ILE   A CG1 1 
ATOM   2022 C  CG2 . ILE   A 1 263 ? -0.823 -9.624  42.880  1.00 43.31  ? 956  ILE   A CG2 1 
ATOM   2023 C  CD1 . ILE   A 1 263 ? 0.789  -10.465 45.314  1.00 45.50  ? 956  ILE   A CD1 1 
ATOM   2024 N  N   . ASP   A 1 264 ? 1.515  -8.001  40.333  1.00 43.66  ? 957  ASP   A N   1 
ATOM   2025 C  CA  . ASP   A 1 264 ? 1.309  -7.897  38.888  1.00 44.84  ? 957  ASP   A CA  1 
ATOM   2026 C  C   . ASP   A 1 264 ? 2.561  -8.328  38.157  1.00 45.24  ? 957  ASP   A C   1 
ATOM   2027 O  O   . ASP   A 1 264 ? 3.566  -7.615  38.191  1.00 45.09  ? 957  ASP   A O   1 
ATOM   2028 C  CB  . ASP   A 1 264 ? 0.872  -6.502  38.428  1.00 47.01  ? 957  ASP   A CB  1 
ATOM   2029 C  CG  . ASP   A 1 264 ? 0.473  -6.510  36.962  1.00 52.25  ? 957  ASP   A CG  1 
ATOM   2030 O  OD1 . ASP   A 1 264 ? -0.098 -7.533  36.506  1.00 53.54  ? 957  ASP   A OD1 1 
ATOM   2031 O  OD2 . ASP   A 1 264 ? 0.762  -5.517  36.261  1.00 54.14  ? 957  ASP   A OD2 1 
ATOM   2032 N  N   . ALA   A 1 265 ? 2.486  -9.493  37.490  1.00 45.46  ? 958  ALA   A N   1 
ATOM   2033 C  CA  . ALA   A 1 265 ? 3.590  -10.098 36.763  1.00 46.29  ? 958  ALA   A CA  1 
ATOM   2034 C  C   . ALA   A 1 265 ? 4.250  -9.183  35.758  1.00 47.58  ? 958  ALA   A C   1 
ATOM   2035 O  O   . ALA   A 1 265 ? 5.476  -9.120  35.723  1.00 48.06  ? 958  ALA   A O   1 
ATOM   2036 C  CB  . ALA   A 1 265 ? 3.140  -11.377 36.091  1.00 46.36  ? 958  ALA   A CB  1 
ATOM   2037 N  N   . ASP   A 1 266 ? 3.460  -8.442  34.961  1.00 47.91  ? 959  ASP   A N   1 
ATOM   2038 C  CA  . ASP   A 1 266 ? 4.033  -7.555  33.947  1.00 48.43  ? 959  ASP   A CA  1 
ATOM   2039 C  C   . ASP   A 1 266 ? 4.733  -6.329  34.525  1.00 47.87  ? 959  ASP   A C   1 
ATOM   2040 O  O   . ASP   A 1 266 ? 5.535  -5.710  33.827  1.00 48.36  ? 959  ASP   A O   1 
ATOM   2041 C  CB  . ASP   A 1 266 ? 2.985  -7.159  32.901  1.00 51.23  ? 959  ASP   A CB  1 
ATOM   2042 C  CG  . ASP   A 1 266 ? 2.456  -8.354  32.135  1.00 58.50  ? 959  ASP   A CG  1 
ATOM   2043 O  OD1 . ASP   A 1 266 ? 3.231  -9.337  31.942  1.00 59.57  ? 959  ASP   A OD1 1 
ATOM   2044 O  OD2 . ASP   A 1 266 ? 1.266  -8.329  31.747  1.00 61.63  ? 959  ASP   A OD2 1 
ATOM   2045 N  N   . SER   A 1 267 ? 4.453  -5.978  35.783  1.00 46.72  ? 960  SER   A N   1 
ATOM   2046 C  CA  . SER   A 1 267 ? 5.101  -4.836  36.417  1.00 46.33  ? 960  SER   A CA  1 
ATOM   2047 C  C   . SER   A 1 267 ? 6.491  -5.172  36.991  1.00 45.29  ? 960  SER   A C   1 
ATOM   2048 O  O   . SER   A 1 267 ? 7.227  -4.259  37.351  1.00 45.68  ? 960  SER   A O   1 
ATOM   2049 C  CB  . SER   A 1 267 ? 4.210  -4.266  37.511  1.00 48.22  ? 960  SER   A CB  1 
ATOM   2050 O  OG  . SER   A 1 267 ? 2.928  -3.966  36.986  1.00 50.64  ? 960  SER   A OG  1 
ATOM   2051 N  N   . ARG   A 1 268 ? 6.839  -6.463  37.104  1.00 43.87  ? 961  ARG   A N   1 
ATOM   2052 C  CA  . ARG   A 1 268 ? 8.125  -6.904  37.635  1.00 42.84  ? 961  ARG   A CA  1 
ATOM   2053 C  C   . ARG   A 1 268 ? 9.266  -6.513  36.707  1.00 42.98  ? 961  ARG   A C   1 
ATOM   2054 O  O   . ARG   A 1 268 ? 9.076  -6.441  35.489  1.00 43.45  ? 961  ARG   A O   1 
ATOM   2055 C  CB  . ARG   A 1 268 ? 8.115  -8.430  37.814  1.00 42.01  ? 961  ARG   A CB  1 
ATOM   2056 C  CG  . ARG   A 1 268 ? 7.236  -8.902  38.949  1.00 42.02  ? 961  ARG   A CG  1 
ATOM   2057 C  CD  . ARG   A 1 268 ? 7.060  -10.403 38.913  1.00 42.69  ? 961  ARG   A CD  1 
ATOM   2058 N  NE  . ARG   A 1 268 ? 5.910  -10.816 39.716  1.00 43.46  ? 961  ARG   A NE  1 
ATOM   2059 C  CZ  . ARG   A 1 268 ? 5.179  -11.900 39.481  1.00 45.68  ? 961  ARG   A CZ  1 
ATOM   2060 N  NH1 . ARG   A 1 268 ? 5.475  -12.704 38.466  1.00 45.89  ? 961  ARG   A NH1 1 
ATOM   2061 N  NH2 . ARG   A 1 268 ? 4.140  -12.186 40.255  1.00 45.15  ? 961  ARG   A NH2 1 
ATOM   2062 N  N   . PRO   A 1 269 ? 10.477 -6.297  37.257  1.00 42.49  ? 962  PRO   A N   1 
ATOM   2063 C  CA  . PRO   A 1 269 ? 11.617 -5.957  36.392  1.00 42.59  ? 962  PRO   A CA  1 
ATOM   2064 C  C   . PRO   A 1 269 ? 11.931 -7.049  35.377  1.00 43.08  ? 962  PRO   A C   1 
ATOM   2065 O  O   . PRO   A 1 269 ? 11.696 -8.213  35.642  1.00 43.78  ? 962  PRO   A O   1 
ATOM   2066 C  CB  . PRO   A 1 269 ? 12.777 -5.775  37.379  1.00 43.15  ? 962  PRO   A CB  1 
ATOM   2067 C  CG  . PRO   A 1 269 ? 12.340 -6.379  38.647  1.00 43.36  ? 962  PRO   A CG  1 
ATOM   2068 C  CD  . PRO   A 1 269 ? 10.859 -6.318  38.680  1.00 41.78  ? 962  PRO   A CD  1 
ATOM   2069 N  N   . LYS   A 1 270 ? 12.418 -6.675  34.203  1.00 42.79  ? 963  LYS   A N   1 
ATOM   2070 C  CA  . LYS   A 1 270 ? 12.777 -7.643  33.173  1.00 42.95  ? 963  LYS   A CA  1 
ATOM   2071 C  C   . LYS   A 1 270 ? 14.212 -8.093  33.395  1.00 42.62  ? 963  LYS   A C   1 
ATOM   2072 O  O   . LYS   A 1 270 ? 14.995 -7.350  33.985  1.00 42.91  ? 963  LYS   A O   1 
ATOM   2073 C  CB  . LYS   A 1 270 ? 12.617 -7.038  31.766  1.00 45.23  ? 963  LYS   A CB  1 
ATOM   2074 C  CG  . LYS   A 1 270 ? 11.250 -7.294  31.146  1.00 49.93  ? 963  LYS   A CG  1 
ATOM   2075 C  CD  . LYS   A 1 270 ? 10.171 -6.499  31.861  1.00 55.22  ? 963  LYS   A CD  1 
ATOM   2076 C  CE  . LYS   A 1 270 ? 8.791  -7.089  31.752  1.00 59.59  ? 963  LYS   A CE  1 
ATOM   2077 N  NZ  . LYS   A 1 270 ? 7.887  -6.391  32.695  1.00 62.71  ? 963  LYS   A NZ  1 
ATOM   2078 N  N   . PHE   A 1 271 ? 14.584 -9.289  32.899  1.00 42.09  ? 964  PHE   A N   1 
ATOM   2079 C  CA  . PHE   A 1 271 ? 15.961 -9.762  33.048  1.00 42.05  ? 964  PHE   A CA  1 
ATOM   2080 C  C   . PHE   A 1 271 ? 16.961 -8.821  32.380  1.00 42.78  ? 964  PHE   A C   1 
ATOM   2081 O  O   . PHE   A 1 271 ? 18.059 -8.665  32.892  1.00 43.08  ? 964  PHE   A O   1 
ATOM   2082 C  CB  . PHE   A 1 271 ? 16.134 -11.187 32.541  1.00 41.60  ? 964  PHE   A CB  1 
ATOM   2083 C  CG  . PHE   A 1 271 ? 15.485 -12.228 33.420  1.00 42.26  ? 964  PHE   A CG  1 
ATOM   2084 C  CD1 . PHE   A 1 271 ? 15.920 -12.431 34.717  1.00 42.98  ? 964  PHE   A CD1 1 
ATOM   2085 C  CD2 . PHE   A 1 271 ? 14.444 -13.012 32.944  1.00 43.09  ? 964  PHE   A CD2 1 
ATOM   2086 C  CE1 . PHE   A 1 271 ? 15.316 -13.386 35.525  1.00 43.87  ? 964  PHE   A CE1 1 
ATOM   2087 C  CE2 . PHE   A 1 271 ? 13.840 -13.965 33.752  1.00 43.70  ? 964  PHE   A CE2 1 
ATOM   2088 C  CZ  . PHE   A 1 271 ? 14.283 -14.150 35.034  1.00 43.69  ? 964  PHE   A CZ  1 
ATOM   2089 N  N   . ARG   A 1 272 ? 16.552 -8.147  31.286  1.00 42.96  ? 965  ARG   A N   1 
ATOM   2090 C  CA  . ARG   A 1 272 ? 17.339 -7.163  30.542  1.00 43.41  ? 965  ARG   A CA  1 
ATOM   2091 C  C   . ARG   A 1 272 ? 17.687 -5.986  31.474  1.00 42.34  ? 965  ARG   A C   1 
ATOM   2092 O  O   . ARG   A 1 272 ? 18.843 -5.568  31.540  1.00 42.52  ? 965  ARG   A O   1 
ATOM   2093 C  CB  . ARG   A 1 272 ? 16.509 -6.654  29.344  1.00 46.51  ? 965  ARG   A CB  1 
ATOM   2094 C  CG  . ARG   A 1 272 ? 17.294 -6.348  28.082  1.00 53.27  ? 965  ARG   A CG  1 
ATOM   2095 C  CD  . ARG   A 1 272 ? 17.551 -4.863  27.867  1.00 60.62  ? 965  ARG   A CD  1 
ATOM   2096 N  NE  . ARG   A 1 272 ? 18.544 -4.603  26.818  1.00 67.21  ? 965  ARG   A NE  1 
ATOM   2097 C  CZ  . ARG   A 1 272 ? 19.865 -4.659  26.995  1.00 71.89  ? 965  ARG   A CZ  1 
ATOM   2098 N  NH1 . ARG   A 1 272 ? 20.372 -4.991  28.180  1.00 71.97  ? 965  ARG   A NH1 1 
ATOM   2099 N  NH2 . ARG   A 1 272 ? 20.686 -4.406  25.985  1.00 72.79  ? 965  ARG   A NH2 1 
ATOM   2100 N  N   . GLU   A 1 273 ? 16.685 -5.483  32.209  1.00 40.90  ? 966  GLU   A N   1 
ATOM   2101 C  CA  . GLU   A 1 273 ? 16.818 -4.379  33.152  1.00 40.05  ? 966  GLU   A CA  1 
ATOM   2102 C  C   . GLU   A 1 273 ? 17.635 -4.783  34.385  1.00 38.95  ? 966  GLU   A C   1 
ATOM   2103 O  O   . GLU   A 1 273 ? 18.376 -3.962  34.931  1.00 39.31  ? 966  GLU   A O   1 
ATOM   2104 C  CB  . GLU   A 1 273 ? 15.427 -3.924  33.606  1.00 42.01  ? 966  GLU   A CB  1 
ATOM   2105 C  CG  . GLU   A 1 273 ? 14.508 -3.503  32.477  1.00 46.84  ? 966  GLU   A CG  1 
ATOM   2106 C  CD  . GLU   A 1 273 ? 13.053 -3.317  32.864  1.00 55.46  ? 966  GLU   A CD  1 
ATOM   2107 O  OE1 . GLU   A 1 273 ? 12.247 -2.966  31.972  1.00 58.39  ? 966  GLU   A OE1 1 
ATOM   2108 O  OE2 . GLU   A 1 273 ? 12.708 -3.546  34.047  1.00 57.81  ? 966  GLU   A OE2 1 
ATOM   2109 N  N   . LEU   A 1 274 ? 17.476 -6.034  34.834  1.00 37.51  ? 967  LEU   A N   1 
ATOM   2110 C  CA  . LEU   A 1 274 ? 18.193 -6.574  35.980  1.00 37.23  ? 967  LEU   A CA  1 
ATOM   2111 C  C   . LEU   A 1 274 ? 19.696 -6.657  35.711  1.00 37.63  ? 967  LEU   A C   1 
ATOM   2112 O  O   . LEU   A 1 274 ? 20.496 -6.393  36.605  1.00 38.26  ? 967  LEU   A O   1 
ATOM   2113 C  CB  . LEU   A 1 274 ? 17.620 -7.947  36.381  1.00 36.66  ? 967  LEU   A CB  1 
ATOM   2114 C  CG  . LEU   A 1 274 ? 16.187 -7.937  36.925  1.00 36.74  ? 967  LEU   A CG  1 
ATOM   2115 C  CD1 . LEU   A 1 274 ? 15.603 -9.336  36.968  1.00 37.24  ? 967  LEU   A CD1 1 
ATOM   2116 C  CD2 . LEU   A 1 274 ? 16.114 -7.276  38.280  1.00 36.22  ? 967  LEU   A CD2 1 
ATOM   2117 N  N   . ILE   A 1 275 ? 20.082 -6.983  34.473  1.00 37.59  ? 968  ILE   A N   1 
ATOM   2118 C  CA  . ILE   A 1 275 ? 21.487 -7.042  34.060  1.00 38.19  ? 968  ILE   A CA  1 
ATOM   2119 C  C   . ILE   A 1 275 ? 22.088 -5.659  34.170  1.00 39.78  ? 968  ILE   A C   1 
ATOM   2120 O  O   . ILE   A 1 275 ? 23.168 -5.514  34.724  1.00 41.05  ? 968  ILE   A O   1 
ATOM   2121 C  CB  . ILE   A 1 275 ? 21.659 -7.578  32.618  1.00 37.96  ? 968  ILE   A CB  1 
ATOM   2122 C  CG1 . ILE   A 1 275 ? 21.146 -9.010  32.457  1.00 37.99  ? 968  ILE   A CG1 1 
ATOM   2123 C  CG2 . ILE   A 1 275 ? 23.104 -7.485  32.184  1.00 38.41  ? 968  ILE   A CG2 1 
ATOM   2124 C  CD1 . ILE   A 1 275 ? 20.957 -9.428  30.982  1.00 38.52  ? 968  ILE   A CD1 1 
ATOM   2125 N  N   . ILE   A 1 276 ? 21.376 -4.640  33.694  1.00 39.96  ? 969  ILE   A N   1 
ATOM   2126 C  CA  . ILE   A 1 276 ? 21.848 -3.260  33.753  1.00 40.77  ? 969  ILE   A CA  1 
ATOM   2127 C  C   . ILE   A 1 276 ? 21.956 -2.736  35.194  1.00 41.35  ? 969  ILE   A C   1 
ATOM   2128 O  O   . ILE   A 1 276 ? 23.009 -2.214  35.570  1.00 41.76  ? 969  ILE   A O   1 
ATOM   2129 C  CB  . ILE   A 1 276 ? 20.968 -2.361  32.846  1.00 41.44  ? 969  ILE   A CB  1 
ATOM   2130 C  CG1 . ILE   A 1 276 ? 21.098 -2.791  31.381  1.00 42.72  ? 969  ILE   A CG1 1 
ATOM   2131 C  CG2 . ILE   A 1 276 ? 21.323 -0.891  33.005  1.00 41.83  ? 969  ILE   A CG2 1 
ATOM   2132 C  CD1 . ILE   A 1 276 ? 19.908 -2.376  30.501  1.00 44.30  ? 969  ILE   A CD1 1 
ATOM   2133 N  N   . GLU   A 1 277 ? 20.902 -2.902  36.007  1.00 41.19  ? 970  GLU   A N   1 
ATOM   2134 C  CA  . GLU   A 1 277 ? 20.934 -2.425  37.389  1.00 41.63  ? 970  GLU   A CA  1 
ATOM   2135 C  C   . GLU   A 1 277 ? 22.063 -3.053  38.198  1.00 40.66  ? 970  GLU   A C   1 
ATOM   2136 O  O   . GLU   A 1 277 ? 22.824 -2.330  38.840  1.00 41.10  ? 970  GLU   A O   1 
ATOM   2137 C  CB  . GLU   A 1 277 ? 19.588 -2.645  38.094  1.00 45.78  ? 970  GLU   A CB  1 
ATOM   2138 C  CG  . GLU   A 1 277 ? 18.770 -1.376  38.265  1.00 55.59  ? 970  GLU   A CG  1 
ATOM   2139 C  CD  . GLU   A 1 277 ? 19.461 -0.221  38.976  1.00 68.20  ? 970  GLU   A CD  1 
ATOM   2140 O  OE1 . GLU   A 1 277 ? 19.684 -0.316  40.208  1.00 70.18  ? 970  GLU   A OE1 1 
ATOM   2141 O  OE2 . GLU   A 1 277 ? 19.759 0.793   38.300  1.00 72.30  ? 970  GLU   A OE2 1 
ATOM   2142 N  N   . PHE   A 1 278 ? 22.191 -4.389  38.152  1.00 38.96  ? 971  PHE   A N   1 
ATOM   2143 C  CA  . PHE   A 1 278 ? 23.234 -5.081  38.900  1.00 37.82  ? 971  PHE   A CA  1 
ATOM   2144 C  C   . PHE   A 1 278 ? 24.634 -4.819  38.341  1.00 37.87  ? 971  PHE   A C   1 
ATOM   2145 O  O   . PHE   A 1 278 ? 25.598 -4.902  39.092  1.00 37.75  ? 971  PHE   A O   1 
ATOM   2146 C  CB  . PHE   A 1 278 ? 22.928 -6.577  39.032  1.00 36.82  ? 971  PHE   A CB  1 
ATOM   2147 C  CG  . PHE   A 1 278 ? 21.919 -6.910  40.109  1.00 36.44  ? 971  PHE   A CG  1 
ATOM   2148 C  CD1 . PHE   A 1 278 ? 22.241 -6.781  41.449  1.00 36.66  ? 971  PHE   A CD1 1 
ATOM   2149 C  CD2 . PHE   A 1 278 ? 20.657 -7.377  39.780  1.00 36.73  ? 971  PHE   A CD2 1 
ATOM   2150 C  CE1 . PHE   A 1 278 ? 21.314 -7.102  42.437  1.00 37.05  ? 971  PHE   A CE1 1 
ATOM   2151 C  CE2 . PHE   A 1 278 ? 19.729 -7.689  40.772  1.00 36.80  ? 971  PHE   A CE2 1 
ATOM   2152 C  CZ  . PHE   A 1 278 ? 20.064 -7.552  42.090  1.00 36.45  ? 971  PHE   A CZ  1 
ATOM   2153 N  N   . SER   A 1 279 ? 24.754 -4.471  37.046  1.00 38.00  ? 972  SER   A N   1 
ATOM   2154 C  CA  . SER   A 1 279 ? 26.043 -4.119  36.438  1.00 38.66  ? 972  SER   A CA  1 
ATOM   2155 C  C   . SER   A 1 279 ? 26.484 -2.743  36.941  1.00 39.24  ? 972  SER   A C   1 
ATOM   2156 O  O   . SER   A 1 279 ? 27.646 -2.571  37.284  1.00 39.39  ? 972  SER   A O   1 
ATOM   2157 C  CB  . SER   A 1 279 ? 25.950 -4.111  34.914  1.00 39.75  ? 972  SER   A CB  1 
ATOM   2158 O  OG  . SER   A 1 279 ? 25.747 -5.428  34.424  1.00 41.79  ? 972  SER   A OG  1 
ATOM   2159 N  N   . LYS   A 1 280 ? 25.546 -1.788  37.041  1.00 39.53  ? 973  LYS   A N   1 
ATOM   2160 C  CA  . LYS   A 1 280 ? 25.794 -0.459  37.592  1.00 41.40  ? 973  LYS   A CA  1 
ATOM   2161 C  C   . LYS   A 1 280 ? 26.255 -0.610  39.057  1.00 42.31  ? 973  LYS   A C   1 
ATOM   2162 O  O   . LYS   A 1 280 ? 27.268 -0.046  39.454  1.00 42.26  ? 973  LYS   A O   1 
ATOM   2163 C  CB  . LYS   A 1 280 ? 24.500 0.392   37.482  1.00 45.11  ? 973  LYS   A CB  1 
ATOM   2164 C  CG  . LYS   A 1 280 ? 24.421 1.633   38.383  1.00 51.95  ? 973  LYS   A CG  1 
ATOM   2165 C  CD  . LYS   A 1 280 ? 22.957 1.908   38.828  1.00 57.67  ? 973  LYS   A CD  1 
ATOM   2166 C  CE  . LYS   A 1 280 ? 22.783 2.946   39.926  1.00 61.29  ? 973  LYS   A CE  1 
ATOM   2167 N  NZ  . LYS   A 1 280 ? 23.061 4.338   39.458  1.00 63.31  ? 973  LYS   A NZ  1 
ATOM   2168 N  N   . MET   A 1 281 ? 25.563 -1.449  39.817  1.00 43.29  ? 974  MET   A N   1 
ATOM   2169 C  CA  . MET   A 1 281 ? 25.917 -1.722  41.200  1.00 44.76  ? 974  MET   A CA  1 
ATOM   2170 C  C   . MET   A 1 281 ? 27.274 -2.402  41.364  1.00 46.34  ? 974  MET   A C   1 
ATOM   2171 O  O   . MET   A 1 281 ? 28.000 -2.066  42.295  1.00 46.88  ? 974  MET   A O   1 
ATOM   2172 C  CB  . MET   A 1 281 ? 24.819 -2.537  41.888  1.00 44.64  ? 974  MET   A CB  1 
ATOM   2173 C  CG  . MET   A 1 281 ? 23.571 -1.746  42.110  1.00 45.51  ? 974  MET   A CG  1 
ATOM   2174 S  SD  . MET   A 1 281 ? 22.314 -2.706  42.928  1.00 47.45  ? 974  MET   A SD  1 
ATOM   2175 C  CE  . MET   A 1 281 ? 21.134 -1.475  43.237  1.00 45.69  ? 974  MET   A CE  1 
ATOM   2176 N  N   . ALA   A 1 282 ? 27.630 -3.338  40.469  1.00 46.70  ? 975  ALA   A N   1 
ATOM   2177 C  CA  . ALA   A 1 282 ? 28.916 -4.030  40.569  1.00 47.63  ? 975  ALA   A CA  1 
ATOM   2178 C  C   . ALA   A 1 282 ? 30.128 -3.166  40.200  1.00 48.83  ? 975  ALA   A C   1 
ATOM   2179 O  O   . ALA   A 1 282 ? 31.257 -3.626  40.340  1.00 49.22  ? 975  ALA   A O   1 
ATOM   2180 C  CB  . ALA   A 1 282 ? 28.905 -5.318  39.764  1.00 47.72  ? 975  ALA   A CB  1 
ATOM   2181 N  N   . ARG   A 1 283 ? 29.907 -1.920  39.758  1.00 49.45  ? 976  ARG   A N   1 
ATOM   2182 C  CA  . ARG   A 1 283 ? 31.002 -0.993  39.463  1.00 50.80  ? 976  ARG   A CA  1 
ATOM   2183 C  C   . ARG   A 1 283 ? 31.485 -0.264  40.733  1.00 51.63  ? 976  ARG   A C   1 
ATOM   2184 O  O   . ARG   A 1 283 ? 32.658 0.089   40.828  1.00 52.01  ? 976  ARG   A O   1 
ATOM   2185 C  CB  . ARG   A 1 283 ? 30.643 -0.030  38.325  1.00 52.21  ? 976  ARG   A CB  1 
ATOM   2186 C  CG  . ARG   A 1 283 ? 30.491 -0.783  37.012  1.00 55.95  ? 976  ARG   A CG  1 
ATOM   2187 C  CD  . ARG   A 1 283 ? 30.577 0.111   35.797  1.00 60.05  ? 976  ARG   A CD  1 
ATOM   2188 N  NE  . ARG   A 1 283 ? 29.361 0.899   35.577  1.00 63.99  ? 976  ARG   A NE  1 
ATOM   2189 C  CZ  . ARG   A 1 283 ? 28.288 0.463   34.918  1.00 67.15  ? 976  ARG   A CZ  1 
ATOM   2190 N  NH1 . ARG   A 1 283 ? 27.243 1.259   34.739  1.00 67.62  ? 976  ARG   A NH1 1 
ATOM   2191 N  NH2 . ARG   A 1 283 ? 28.253 -0.773  34.434  1.00 67.12  ? 976  ARG   A NH2 1 
ATOM   2192 N  N   . ASP   A 1 284 ? 30.599 -0.087  41.720  1.00 51.64  ? 977  ASP   A N   1 
ATOM   2193 C  CA  . ASP   A 1 284 ? 30.932 0.472   43.030  1.00 52.16  ? 977  ASP   A CA  1 
ATOM   2194 C  C   . ASP   A 1 284 ? 30.295 -0.497  44.042  1.00 51.88  ? 977  ASP   A C   1 
ATOM   2195 O  O   . ASP   A 1 284 ? 29.256 -0.187  44.622  1.00 52.22  ? 977  ASP   A O   1 
ATOM   2196 C  CB  . ASP   A 1 284 ? 30.352 1.894   43.187  1.00 54.48  ? 977  ASP   A CB  1 
ATOM   2197 C  CG  . ASP   A 1 284 ? 31.005 2.735   44.283  1.00 59.53  ? 977  ASP   A CG  1 
ATOM   2198 O  OD1 . ASP   A 1 284 ? 31.800 2.175   45.072  1.00 60.35  ? 977  ASP   A OD1 1 
ATOM   2199 O  OD2 . ASP   A 1 284 ? 30.723 3.955   44.349  1.00 61.49  ? 977  ASP   A OD2 1 
ATOM   2200 N  N   . PRO   A 1 285 ? 30.857 -1.716  44.181  1.00 51.07  ? 978  PRO   A N   1 
ATOM   2201 C  CA  . PRO   A 1 285 ? 30.228 -2.731  45.036  1.00 50.71  ? 978  PRO   A CA  1 
ATOM   2202 C  C   . PRO   A 1 285 ? 30.011 -2.375  46.495  1.00 50.64  ? 978  PRO   A C   1 
ATOM   2203 O  O   . PRO   A 1 285 ? 28.957 -2.715  47.027  1.00 50.89  ? 978  PRO   A O   1 
ATOM   2204 C  CB  . PRO   A 1 285 ? 31.165 -3.934  44.912  1.00 51.37  ? 978  PRO   A CB  1 
ATOM   2205 C  CG  . PRO   A 1 285 ? 31.887 -3.728  43.655  1.00 51.85  ? 978  PRO   A CG  1 
ATOM   2206 C  CD  . PRO   A 1 285 ? 32.057 -2.253  43.515  1.00 50.38  ? 978  PRO   A CD  1 
ATOM   2207 N  N   . GLN   A 1 286 ? 30.988 -1.736  47.157  1.00 50.17  ? 979  GLN   A N   1 
ATOM   2208 C  CA  . GLN   A 1 286 ? 30.836 -1.395  48.574  1.00 50.26  ? 979  GLN   A CA  1 
ATOM   2209 C  C   . GLN   A 1 286 ? 29.753 -0.358  48.850  1.00 49.88  ? 979  GLN   A C   1 
ATOM   2210 O  O   . GLN   A 1 286 ? 29.321 -0.230  49.997  1.00 50.56  ? 979  GLN   A O   1 
ATOM   2211 C  CB  . GLN   A 1 286 ? 32.158 -0.974  49.207  1.00 52.32  ? 979  GLN   A CB  1 
ATOM   2212 C  CG  . GLN   A 1 286 ? 33.035 -2.143  49.579  1.00 56.70  ? 979  GLN   A CG  1 
ATOM   2213 C  CD  . GLN   A 1 286 ? 34.240 -2.185  48.694  1.00 62.94  ? 979  GLN   A CD  1 
ATOM   2214 O  OE1 . GLN   A 1 286 ? 34.152 -2.508  47.504  1.00 64.97  ? 979  GLN   A OE1 1 
ATOM   2215 N  NE2 . GLN   A 1 286 ? 35.389 -1.842  49.254  1.00 64.19  ? 979  GLN   A NE2 1 
ATOM   2216 N  N   . ARG   A 1 287 ? 29.298 0.367   47.817  1.00 48.85  ? 980  ARG   A N   1 
ATOM   2217 C  CA  . ARG   A 1 287 ? 28.211 1.329   47.981  1.00 48.69  ? 980  ARG   A CA  1 
ATOM   2218 C  C   . ARG   A 1 287 ? 26.879 0.601   48.161  1.00 47.46  ? 980  ARG   A C   1 
ATOM   2219 O  O   . ARG   A 1 287 ? 26.018 1.068   48.908  1.00 47.83  ? 980  ARG   A O   1 
ATOM   2220 C  CB  . ARG   A 1 287 ? 28.113 2.281   46.769  1.00 50.97  ? 980  ARG   A CB  1 
ATOM   2221 C  CG  . ARG   A 1 287 ? 27.182 3.458   47.020  1.00 56.30  ? 980  ARG   A CG  1 
ATOM   2222 C  CD  . ARG   A 1 287 ? 26.567 4.053   45.765  1.00 62.90  ? 980  ARG   A CD  1 
ATOM   2223 N  NE  . ARG   A 1 287 ? 27.540 4.742   44.911  1.00 69.65  ? 980  ARG   A NE  1 
ATOM   2224 C  CZ  . ARG   A 1 287 ? 27.667 4.535   43.598  1.00 74.28  ? 980  ARG   A CZ  1 
ATOM   2225 N  NH1 . ARG   A 1 287 ? 26.904 3.637   42.981  1.00 74.95  ? 980  ARG   A NH1 1 
ATOM   2226 N  NH2 . ARG   A 1 287 ? 28.574 5.207   42.898  1.00 74.27  ? 980  ARG   A NH2 1 
ATOM   2227 N  N   . TYR   A 1 288 ? 26.725 -0.566  47.513  1.00 45.81  ? 981  TYR   A N   1 
ATOM   2228 C  CA  . TYR   A 1 288 ? 25.465 -1.281  47.511  1.00 44.42  ? 981  TYR   A CA  1 
ATOM   2229 C  C   . TYR   A 1 288 ? 25.395 -2.461  48.480  1.00 43.68  ? 981  TYR   A C   1 
ATOM   2230 O  O   . TYR   A 1 288 ? 24.302 -2.786  48.940  1.00 43.71  ? 981  TYR   A O   1 
ATOM   2231 C  CB  . TYR   A 1 288 ? 25.129 -1.680  46.082  1.00 43.74  ? 981  TYR   A CB  1 
ATOM   2232 C  CG  . TYR   A 1 288 ? 24.935 -0.445  45.230  1.00 43.78  ? 981  TYR   A CG  1 
ATOM   2233 C  CD1 . TYR   A 1 288 ? 23.839 0.383   45.414  1.00 44.33  ? 981  TYR   A CD1 1 
ATOM   2234 C  CD2 . TYR   A 1 288 ? 25.919 -0.023  44.353  1.00 44.44  ? 981  TYR   A CD2 1 
ATOM   2235 C  CE1 . TYR   A 1 288 ? 23.685 1.552   44.684  1.00 44.88  ? 981  TYR   A CE1 1 
ATOM   2236 C  CE2 . TYR   A 1 288 ? 25.772 1.139   43.606  1.00 45.11  ? 981  TYR   A CE2 1 
ATOM   2237 C  CZ  . TYR   A 1 288 ? 24.646 1.918   43.767  1.00 45.96  ? 981  TYR   A CZ  1 
ATOM   2238 O  OH  . TYR   A 1 288 ? 24.480 3.062   43.027  1.00 48.17  ? 981  TYR   A OH  1 
ATOM   2239 N  N   . LEU   A 1 289 ? 26.526 -3.070  48.830  1.00 42.98  ? 982  LEU   A N   1 
ATOM   2240 C  CA  . LEU   A 1 289 ? 26.520 -4.156  49.810  1.00 42.88  ? 982  LEU   A CA  1 
ATOM   2241 C  C   . LEU   A 1 289 ? 27.499 -3.845  50.922  1.00 43.81  ? 982  LEU   A C   1 
ATOM   2242 O  O   . LEU   A 1 289 ? 28.657 -3.510  50.660  1.00 43.89  ? 982  LEU   A O   1 
ATOM   2243 C  CB  . LEU   A 1 289 ? 26.804 -5.538  49.196  1.00 42.06  ? 982  LEU   A CB  1 
ATOM   2244 C  CG  . LEU   A 1 289 ? 25.752 -6.131  48.276  1.00 42.15  ? 982  LEU   A CG  1 
ATOM   2245 C  CD1 . LEU   A 1 289 ? 26.159 -7.496  47.825  1.00 42.48  ? 982  LEU   A CD1 1 
ATOM   2246 C  CD2 . LEU   A 1 289 ? 24.410 -6.221  48.948  1.00 42.59  ? 982  LEU   A CD2 1 
ATOM   2247 N  N   . VAL   A 1 290 ? 27.025 -3.937  52.169  1.00 44.17  ? 983  VAL   A N   1 
ATOM   2248 C  CA  . VAL   A 1 290 ? 27.828 -3.655  53.349  1.00 44.94  ? 983  VAL   A CA  1 
ATOM   2249 C  C   . VAL   A 1 290 ? 28.213 -4.965  54.018  1.00 45.58  ? 983  VAL   A C   1 
ATOM   2250 O  O   . VAL   A 1 290 ? 27.425 -5.547  54.767  1.00 45.39  ? 983  VAL   A O   1 
ATOM   2251 C  CB  . VAL   A 1 290 ? 27.097 -2.697  54.320  1.00 45.68  ? 983  VAL   A CB  1 
ATOM   2252 C  CG1 . VAL   A 1 290 ? 28.003 -2.312  55.480  1.00 46.25  ? 983  VAL   A CG1 1 
ATOM   2253 C  CG2 . VAL   A 1 290 ? 26.591 -1.453  53.589  1.00 45.87  ? 983  VAL   A CG2 1 
ATOM   2254 N  N   . ILE   A 1 291 ? 29.423 -5.444  53.716  1.00 46.37  ? 984  ILE   A N   1 
ATOM   2255 C  CA  . ILE   A 1 291 ? 29.956 -6.697  54.245  1.00 47.97  ? 984  ILE   A CA  1 
ATOM   2256 C  C   . ILE   A 1 291 ? 31.229 -6.417  55.037  1.00 49.86  ? 984  ILE   A C   1 
ATOM   2257 O  O   . ILE   A 1 291 ? 32.065 -5.634  54.586  1.00 49.74  ? 984  ILE   A O   1 
ATOM   2258 C  CB  . ILE   A 1 291 ? 30.230 -7.675  53.077  1.00 48.32  ? 984  ILE   A CB  1 
ATOM   2259 C  CG1 . ILE   A 1 291 ? 28.937 -8.027  52.342  1.00 49.22  ? 984  ILE   A CG1 1 
ATOM   2260 C  CG2 . ILE   A 1 291 ? 30.957 -8.929  53.550  1.00 48.75  ? 984  ILE   A CG2 1 
ATOM   2261 C  CD1 . ILE   A 1 291 ? 29.155 -8.542  51.035  1.00 50.68  ? 984  ILE   A CD1 1 
ATOM   2262 N  N   . GLN   A 1 292 ? 31.386 -7.066  56.209  1.00 51.42  ? 985  GLN   A N   1 
ATOM   2263 C  CA  . GLN   A 1 292 ? 32.568 -6.878  57.053  1.00 53.18  ? 985  GLN   A CA  1 
ATOM   2264 C  C   . GLN   A 1 292 ? 33.825 -7.384  56.381  1.00 53.96  ? 985  GLN   A C   1 
ATOM   2265 O  O   . GLN   A 1 292 ? 33.903 -8.561  56.020  1.00 54.45  ? 985  GLN   A O   1 
ATOM   2266 C  CB  . GLN   A 1 292 ? 32.404 -7.582  58.400  1.00 55.54  ? 985  GLN   A CB  1 
ATOM   2267 C  CG  . GLN   A 1 292 ? 33.536 -7.235  59.355  1.00 60.57  ? 985  GLN   A CG  1 
ATOM   2268 C  CD  . GLN   A 1 292 ? 33.472 -8.022  60.633  1.00 66.50  ? 985  GLN   A CD  1 
ATOM   2269 O  OE1 . GLN   A 1 292 ? 32.897 -9.121  60.692  1.00 68.90  ? 985  GLN   A OE1 1 
ATOM   2270 N  NE2 . GLN   A 1 292 ? 34.077 -7.478  61.684  1.00 66.71  ? 985  GLN   A NE2 1 
ATOM   2271 N  N   . GLY   A 1 293 ? 34.791 -6.498  56.217  1.00 53.98  ? 986  GLY   A N   1 
ATOM   2272 C  CA  . GLY   A 1 293 ? 36.038 -6.871  55.580  1.00 54.93  ? 986  GLY   A CA  1 
ATOM   2273 C  C   . GLY   A 1 293 ? 36.005 -6.703  54.082  1.00 55.94  ? 986  GLY   A C   1 
ATOM   2274 O  O   . GLY   A 1 293 ? 36.289 -7.642  53.348  1.00 56.17  ? 986  GLY   A O   1 
ATOM   2275 N  N   . ASP   A 1 294 ? 35.659 -5.512  53.618  1.00 56.78  ? 987  ASP   A N   1 
ATOM   2276 C  CA  . ASP   A 1 294 ? 35.601 -5.224  52.187  1.00 58.05  ? 987  ASP   A CA  1 
ATOM   2277 C  C   . ASP   A 1 294 ? 36.439 -3.992  51.817  1.00 58.85  ? 987  ASP   A C   1 
ATOM   2278 O  O   . ASP   A 1 294 ? 36.932 -3.269  52.690  1.00 59.34  ? 987  ASP   A O   1 
ATOM   2279 C  CB  . ASP   A 1 294 ? 34.145 -5.041  51.731  1.00 60.03  ? 987  ASP   A CB  1 
ATOM   2280 C  CG  . ASP   A 1 294 ? 33.640 -6.092  50.753  1.00 64.91  ? 987  ASP   A CG  1 
ATOM   2281 O  OD1 . ASP   A 1 294 ? 34.359 -7.084  50.518  1.00 65.59  ? 987  ASP   A OD1 1 
ATOM   2282 O  OD2 . ASP   A 1 294 ? 32.527 -5.922  50.229  1.00 67.31  ? 987  ASP   A OD2 1 
ATOM   2283 N  N   . LEU   B 1 10  ? 20.698 1.857   24.713  1.00 70.91  ? 703  LEU   B N   1 
ATOM   2284 C  CA  . LEU   B 1 10  ? 21.231 0.664   24.050  1.00 71.40  ? 703  LEU   B CA  1 
ATOM   2285 C  C   . LEU   B 1 10  ? 22.577 0.971   23.366  1.00 71.17  ? 703  LEU   B C   1 
ATOM   2286 O  O   . LEU   B 1 10  ? 23.509 0.167   23.430  1.00 71.19  ? 703  LEU   B O   1 
ATOM   2287 C  CB  . LEU   B 1 10  ? 20.201 0.132   23.042  1.00 71.97  ? 703  LEU   B CB  1 
ATOM   2288 C  CG  . LEU   B 1 10  ? 20.559 -1.137  22.271  1.00 73.88  ? 703  LEU   B CG  1 
ATOM   2289 C  CD1 . LEU   B 1 10  ? 20.966 -2.281  23.212  1.00 74.48  ? 703  LEU   B CD1 1 
ATOM   2290 C  CD2 . LEU   B 1 10  ? 19.407 -1.559  21.359  1.00 74.52  ? 703  LEU   B CD2 1 
ATOM   2291 N  N   . LEU   B 1 11  ? 22.678 2.156   22.739  1.00 70.57  ? 704  LEU   B N   1 
ATOM   2292 C  CA  . LEU   B 1 11  ? 23.900 2.634   22.088  1.00 70.07  ? 704  LEU   B CA  1 
ATOM   2293 C  C   . LEU   B 1 11  ? 24.130 4.085   22.484  1.00 69.14  ? 704  LEU   B C   1 
ATOM   2294 O  O   . LEU   B 1 11  ? 23.269 4.933   22.265  1.00 69.16  ? 704  LEU   B O   1 
ATOM   2295 C  CB  . LEU   B 1 11  ? 23.793 2.518   20.561  1.00 70.32  ? 704  LEU   B CB  1 
ATOM   2296 C  CG  . LEU   B 1 11  ? 24.883 3.197   19.730  1.00 71.23  ? 704  LEU   B CG  1 
ATOM   2297 C  CD1 . LEU   B 1 11  ? 26.122 2.331   19.628  1.00 71.73  ? 704  LEU   B CD1 1 
ATOM   2298 C  CD2 . LEU   B 1 11  ? 24.368 3.556   18.379  1.00 71.40  ? 704  LEU   B CD2 1 
ATOM   2299 N  N   . ARG   B 1 12  ? 25.304 4.369   23.028  1.00 68.34  ? 705  ARG   B N   1 
ATOM   2300 C  CA  . ARG   B 1 12  ? 25.668 5.698   23.488  1.00 68.24  ? 705  ARG   B CA  1 
ATOM   2301 C  C   . ARG   B 1 12  ? 26.086 6.636   22.333  1.00 67.05  ? 705  ARG   B C   1 
ATOM   2302 O  O   . ARG   B 1 12  ? 26.852 6.223   21.470  1.00 67.10  ? 705  ARG   B O   1 
ATOM   2303 C  CB  . ARG   B 1 12  ? 26.813 5.555   24.510  1.00 70.56  ? 705  ARG   B CB  1 
ATOM   2304 C  CG  . ARG   B 1 12  ? 26.893 6.681   25.527  1.00 76.37  ? 705  ARG   B CG  1 
ATOM   2305 C  CD  . ARG   B 1 12  ? 27.356 6.197   26.897  1.00 81.97  ? 705  ARG   B CD  1 
ATOM   2306 N  NE  . ARG   B 1 12  ? 26.320 5.414   27.583  1.00 86.72  ? 705  ARG   B NE  1 
ATOM   2307 C  CZ  . ARG   B 1 12  ? 26.534 4.245   28.181  1.00 89.96  ? 705  ARG   B CZ  1 
ATOM   2308 N  NH1 . ARG   B 1 12  ? 25.535 3.600   28.769  1.00 89.54  ? 705  ARG   B NH1 1 
ATOM   2309 N  NH2 . ARG   B 1 12  ? 27.752 3.714   28.199  1.00 90.77  ? 705  ARG   B NH2 1 
ATOM   2310 N  N   . ILE   B 1 13  ? 25.576 7.889   22.303  1.00 65.72  ? 706  ILE   B N   1 
ATOM   2311 C  CA  . ILE   B 1 13  ? 26.026 8.880   21.328  1.00 64.80  ? 706  ILE   B CA  1 
ATOM   2312 C  C   . ILE   B 1 13  ? 27.063 9.703   22.083  1.00 63.97  ? 706  ILE   B C   1 
ATOM   2313 O  O   . ILE   B 1 13  ? 26.755 10.277  23.124  1.00 64.28  ? 706  ILE   B O   1 
ATOM   2314 C  CB  . ILE   B 1 13  ? 24.908 9.772   20.764  1.00 64.95  ? 706  ILE   B CB  1 
ATOM   2315 C  CG1 . ILE   B 1 13  ? 23.705 8.949   20.260  1.00 65.94  ? 706  ILE   B CG1 1 
ATOM   2316 C  CG2 . ILE   B 1 13  ? 25.468 10.663  19.663  1.00 65.35  ? 706  ILE   B CG2 1 
ATOM   2317 C  CD1 . ILE   B 1 13  ? 23.963 8.056   19.079  1.00 67.57  ? 706  ILE   B CD1 1 
ATOM   2318 N  N   . LEU   B 1 14  ? 28.299 9.705   21.608  1.00 62.95  ? 707  LEU   B N   1 
ATOM   2319 C  CA  . LEU   B 1 14  ? 29.398 10.362  22.306  1.00 62.59  ? 707  LEU   B CA  1 
ATOM   2320 C  C   . LEU   B 1 14  ? 29.709 11.773  21.819  1.00 63.08  ? 707  LEU   B C   1 
ATOM   2321 O  O   . LEU   B 1 14  ? 29.637 12.058  20.625  1.00 63.48  ? 707  LEU   B O   1 
ATOM   2322 C  CB  . LEU   B 1 14  ? 30.657 9.492   22.190  1.00 61.97  ? 707  LEU   B CB  1 
ATOM   2323 C  CG  . LEU   B 1 14  ? 30.905 8.475   23.287  1.00 62.40  ? 707  LEU   B CG  1 
ATOM   2324 C  CD1 . LEU   B 1 14  ? 29.782 7.486   23.393  1.00 62.60  ? 707  LEU   B CD1 1 
ATOM   2325 C  CD2 . LEU   B 1 14  ? 32.181 7.738   23.033  1.00 62.83  ? 707  LEU   B CD2 1 
ATOM   2326 N  N   . LYS   B 1 15  ? 30.080 12.650  22.754  1.00 62.86  ? 708  LYS   B N   1 
ATOM   2327 C  CA  . LYS   B 1 15  ? 30.522 14.013  22.470  1.00 63.02  ? 708  LYS   B CA  1 
ATOM   2328 C  C   . LYS   B 1 15  ? 32.049 13.965  22.360  1.00 62.55  ? 708  LYS   B C   1 
ATOM   2329 O  O   . LYS   B 1 15  ? 32.688 13.184  23.072  1.00 62.20  ? 708  LYS   B O   1 
ATOM   2330 C  CB  . LYS   B 1 15  ? 30.127 14.959  23.613  1.00 65.37  ? 708  LYS   B CB  1 
ATOM   2331 C  CG  . LYS   B 1 15  ? 28.624 15.160  23.756  1.00 70.27  ? 708  LYS   B CG  1 
ATOM   2332 C  CD  . LYS   B 1 15  ? 28.284 15.746  25.126  1.00 75.83  ? 708  LYS   B CD  1 
ATOM   2333 C  CE  . LYS   B 1 15  ? 26.820 16.093  25.272  1.00 80.43  ? 708  LYS   B CE  1 
ATOM   2334 N  NZ  . LYS   B 1 15  ? 25.945 14.929  24.972  1.00 83.63  ? 708  LYS   B NZ  1 
ATOM   2335 N  N   . GLU   B 1 16  ? 32.644 14.787  21.484  1.00 62.46  ? 709  GLU   B N   1 
ATOM   2336 C  CA  . GLU   B 1 16  ? 34.108 14.789  21.313  1.00 63.07  ? 709  GLU   B CA  1 
ATOM   2337 C  C   . GLU   B 1 16  ? 34.873 15.085  22.606  1.00 63.58  ? 709  GLU   B C   1 
ATOM   2338 O  O   . GLU   B 1 16  ? 36.045 14.736  22.730  1.00 63.39  ? 709  GLU   B O   1 
ATOM   2339 C  CB  . GLU   B 1 16  ? 34.533 15.784  20.230  1.00 65.30  ? 709  GLU   B CB  1 
ATOM   2340 C  CG  . GLU   B 1 16  ? 33.787 15.636  18.919  1.00 69.78  ? 709  GLU   B CG  1 
ATOM   2341 C  CD  . GLU   B 1 16  ? 34.300 16.567  17.841  1.00 75.22  ? 709  GLU   B CD  1 
ATOM   2342 O  OE1 . GLU   B 1 16  ? 33.565 17.511  17.466  1.00 75.62  ? 709  GLU   B OE1 1 
ATOM   2343 O  OE2 . GLU   B 1 16  ? 35.446 16.356  17.380  1.00 77.09  ? 709  GLU   B OE2 1 
ATOM   2344 N  N   . THR   B 1 17  ? 34.197 15.742  23.558  1.00 64.07  ? 710  THR   B N   1 
ATOM   2345 C  CA  . THR   B 1 17  ? 34.686 16.125  24.872  1.00 64.82  ? 710  THR   B CA  1 
ATOM   2346 C  C   . THR   B 1 17  ? 34.823 14.919  25.827  1.00 65.31  ? 710  THR   B C   1 
ATOM   2347 O  O   . THR   B 1 17  ? 35.619 14.980  26.766  1.00 65.68  ? 710  THR   B O   1 
ATOM   2348 C  CB  . THR   B 1 17  ? 33.752 17.206  25.429  1.00 66.21  ? 710  THR   B CB  1 
ATOM   2349 O  OG1 . THR   B 1 17  ? 32.418 16.681  25.477  1.00 67.27  ? 710  THR   B OG1 1 
ATOM   2350 C  CG2 . THR   B 1 17  ? 33.762 18.472  24.574  1.00 66.52  ? 710  THR   B CG2 1 
ATOM   2351 N  N   . GLU   B 1 18  ? 34.052 13.831  25.588  1.00 65.04  ? 711  GLU   B N   1 
ATOM   2352 C  CA  . GLU   B 1 18  ? 34.067 12.624  26.422  1.00 64.94  ? 711  GLU   B CA  1 
ATOM   2353 C  C   . GLU   B 1 18  ? 35.238 11.698  26.152  1.00 65.02  ? 711  GLU   B C   1 
ATOM   2354 O  O   . GLU   B 1 18  ? 35.481 10.807  26.963  1.00 65.05  ? 711  GLU   B O   1 
ATOM   2355 C  CB  . GLU   B 1 18  ? 32.794 11.803  26.215  1.00 66.50  ? 711  GLU   B CB  1 
ATOM   2356 C  CG  . GLU   B 1 18  ? 31.504 12.530  26.504  1.00 70.59  ? 711  GLU   B CG  1 
ATOM   2357 C  CD  . GLU   B 1 18  ? 30.302 11.624  26.328  1.00 75.73  ? 711  GLU   B CD  1 
ATOM   2358 O  OE1 . GLU   B 1 18  ? 30.408 10.427  26.681  1.00 75.72  ? 711  GLU   B OE1 1 
ATOM   2359 O  OE2 . GLU   B 1 18  ? 29.262 12.103  25.818  1.00 77.98  ? 711  GLU   B OE2 1 
ATOM   2360 N  N   . PHE   B 1 19  ? 35.908 11.827  25.000  1.00 64.94  ? 712  PHE   B N   1 
ATOM   2361 C  CA  . PHE   B 1 19  ? 37.001 10.911  24.667  1.00 65.43  ? 712  PHE   B CA  1 
ATOM   2362 C  C   . PHE   B 1 19  ? 38.192 11.594  23.997  1.00 66.83  ? 712  PHE   B C   1 
ATOM   2363 O  O   . PHE   B 1 19  ? 38.050 12.679  23.425  1.00 67.10  ? 712  PHE   B O   1 
ATOM   2364 C  CB  . PHE   B 1 19  ? 36.493 9.724   23.836  1.00 64.57  ? 712  PHE   B CB  1 
ATOM   2365 C  CG  . PHE   B 1 19  ? 35.983 10.089  22.463  1.00 64.17  ? 712  PHE   B CG  1 
ATOM   2366 C  CD1 . PHE   B 1 19  ? 34.685 10.539  22.284  1.00 64.50  ? 712  PHE   B CD1 1 
ATOM   2367 C  CD2 . PHE   B 1 19  ? 36.790 9.953   21.350  1.00 64.45  ? 712  PHE   B CD2 1 
ATOM   2368 C  CE1 . PHE   B 1 19  ? 34.216 10.869  21.023  1.00 64.98  ? 712  PHE   B CE1 1 
ATOM   2369 C  CE2 . PHE   B 1 19  ? 36.316 10.283  20.092  1.00 64.95  ? 712  PHE   B CE2 1 
ATOM   2370 C  CZ  . PHE   B 1 19  ? 35.029 10.730  19.936  1.00 64.74  ? 712  PHE   B CZ  1 
ATOM   2371 N  N   . LYS   B 1 20  ? 39.379 10.972  24.102  1.00 67.48  ? 713  LYS   B N   1 
ATOM   2372 C  CA  . LYS   B 1 20  ? 40.609 11.542  23.560  1.00 68.78  ? 713  LYS   B CA  1 
ATOM   2373 C  C   . LYS   B 1 20  ? 41.470 10.467  22.919  1.00 69.69  ? 713  LYS   B C   1 
ATOM   2374 O  O   . LYS   B 1 20  ? 41.865 9.520   23.595  1.00 70.14  ? 713  LYS   B O   1 
ATOM   2375 C  CB  . LYS   B 1 20  ? 41.414 12.253  24.676  1.00 71.02  ? 713  LYS   B CB  1 
ATOM   2376 C  CG  . LYS   B 1 20  ? 40.846 13.621  25.103  1.00 75.55  ? 713  LYS   B CG  1 
ATOM   2377 C  CD  . LYS   B 1 20  ? 40.764 13.791  26.636  1.00 79.49  ? 713  LYS   B CD  1 
ATOM   2378 C  CE  . LYS   B 1 20  ? 39.512 14.504  27.111  1.00 82.45  ? 713  LYS   B CE  1 
ATOM   2379 N  NZ  . LYS   B 1 20  ? 38.641 13.604  27.923  1.00 84.35  ? 713  LYS   B NZ  1 
ATOM   2380 N  N   . LYS   B 1 21  ? 41.779 10.614  21.628  1.00 69.78  ? 714  LYS   B N   1 
ATOM   2381 C  CA  . LYS   B 1 21  ? 42.633 9.659   20.909  1.00 70.21  ? 714  LYS   B CA  1 
ATOM   2382 C  C   . LYS   B 1 21  ? 44.069 9.887   21.372  1.00 70.73  ? 714  LYS   B C   1 
ATOM   2383 O  O   . LYS   B 1 21  ? 44.516 11.026  21.402  1.00 71.22  ? 714  LYS   B O   1 
ATOM   2384 C  CB  . LYS   B 1 21  ? 42.519 9.870   19.381  1.00 71.46  ? 714  LYS   B CB  1 
ATOM   2385 C  CG  . LYS   B 1 21  ? 41.099 10.141  18.887  1.00 75.46  ? 714  LYS   B CG  1 
ATOM   2386 C  CD  . LYS   B 1 21  ? 40.933 11.581  18.451  1.00 79.80  ? 714  LYS   B CD  1 
ATOM   2387 C  CE  . LYS   B 1 21  ? 39.532 11.838  18.011  1.00 83.16  ? 714  LYS   B CE  1 
ATOM   2388 N  NZ  . LYS   B 1 21  ? 39.392 11.577  16.563  1.00 84.87  ? 714  LYS   B NZ  1 
ATOM   2389 N  N   . ILE   B 1 22  ? 44.777 8.833   21.762  1.00 70.57  ? 715  ILE   B N   1 
ATOM   2390 C  CA  . ILE   B 1 22  ? 46.139 8.973   22.273  1.00 70.90  ? 715  ILE   B CA  1 
ATOM   2391 C  C   . ILE   B 1 22  ? 47.219 8.522   21.268  1.00 71.43  ? 715  ILE   B C   1 
ATOM   2392 O  O   . ILE   B 1 22  ? 48.077 9.327   20.920  1.00 71.51  ? 715  ILE   B O   1 
ATOM   2393 C  CB  . ILE   B 1 22  ? 46.251 8.262   23.640  1.00 71.02  ? 715  ILE   B CB  1 
ATOM   2394 C  CG1 . ILE   B 1 22  ? 45.382 8.992   24.674  1.00 71.75  ? 715  ILE   B CG1 1 
ATOM   2395 C  CG2 . ILE   B 1 22  ? 47.700 8.130   24.107  1.00 71.29  ? 715  ILE   B CG2 1 
ATOM   2396 C  CD1 . ILE   B 1 22  ? 45.108 8.186   25.874  1.00 72.85  ? 715  ILE   B CD1 1 
ATOM   2397 N  N   . LYS   B 1 23  ? 47.188 7.267   20.804  1.00 71.64  ? 716  LYS   B N   1 
ATOM   2398 C  CA  . LYS   B 1 23  ? 48.198 6.766   19.866  1.00 72.43  ? 716  LYS   B CA  1 
ATOM   2399 C  C   . LYS   B 1 23  ? 47.543 6.139   18.642  1.00 73.03  ? 716  LYS   B C   1 
ATOM   2400 O  O   . LYS   B 1 23  ? 46.424 5.647   18.742  1.00 73.43  ? 716  LYS   B O   1 
ATOM   2401 C  CB  . LYS   B 1 23  ? 49.081 5.721   20.566  1.00 74.19  ? 716  LYS   B CB  1 
ATOM   2402 C  CG  . LYS   B 1 23  ? 50.478 5.559   19.976  1.00 78.56  ? 716  LYS   B CG  1 
ATOM   2403 C  CD  . LYS   B 1 23  ? 51.358 4.599   20.801  1.00 83.47  ? 716  LYS   B CD  1 
ATOM   2404 C  CE  . LYS   B 1 23  ? 51.538 5.068   22.239  1.00 87.67  ? 716  LYS   B CE  1 
ATOM   2405 N  NZ  . LYS   B 1 23  ? 52.557 4.277   22.986  1.00 89.66  ? 716  LYS   B NZ  1 
ATOM   2406 N  N   . VAL   B 1 24  ? 48.237 6.125   17.495  1.00 72.92  ? 717  VAL   B N   1 
ATOM   2407 C  CA  . VAL   B 1 24  ? 47.685 5.500   16.294  1.00 73.26  ? 717  VAL   B CA  1 
ATOM   2408 C  C   . VAL   B 1 24  ? 48.045 4.017   16.282  1.00 73.81  ? 717  VAL   B C   1 
ATOM   2409 O  O   . VAL   B 1 24  ? 49.220 3.660   16.412  1.00 74.25  ? 717  VAL   B O   1 
ATOM   2410 C  CB  . VAL   B 1 24  ? 48.128 6.202   14.998  1.00 73.57  ? 717  VAL   B CB  1 
ATOM   2411 C  CG1 . VAL   B 1 24  ? 47.532 5.523   13.775  1.00 73.68  ? 717  VAL   B CG1 1 
ATOM   2412 C  CG2 . VAL   B 1 24  ? 47.751 7.673   15.031  1.00 74.21  ? 717  VAL   B CG2 1 
ATOM   2413 N  N   . LEU   B 1 25  ? 47.037 3.151   16.161  1.00 73.23  ? 718  LEU   B N   1 
ATOM   2414 C  CA  . LEU   B 1 25  ? 47.274 1.719   16.107  1.00 72.87  ? 718  LEU   B CA  1 
ATOM   2415 C  C   . LEU   B 1 25  ? 47.476 1.239   14.674  1.00 72.40  ? 718  LEU   B C   1 
ATOM   2416 O  O   . LEU   B 1 25  ? 48.271 0.336   14.437  1.00 72.61  ? 718  LEU   B O   1 
ATOM   2417 C  CB  . LEU   B 1 25  ? 46.137 0.951   16.785  1.00 73.10  ? 718  LEU   B CB  1 
ATOM   2418 C  CG  . LEU   B 1 25  ? 45.887 1.298   18.256  1.00 74.51  ? 718  LEU   B CG  1 
ATOM   2419 C  CD1 . LEU   B 1 25  ? 44.727 0.507   18.808  1.00 74.99  ? 718  LEU   B CD1 1 
ATOM   2420 C  CD2 . LEU   B 1 25  ? 47.112 1.047   19.097  1.00 75.27  ? 718  LEU   B CD2 1 
ATOM   2421 N  N   . GLY   B 1 26  ? 46.774 1.842   13.731  1.00 71.82  ? 719  GLY   B N   1 
ATOM   2422 C  CA  . GLY   B 1 26  ? 46.887 1.465   12.332  1.00 72.16  ? 719  GLY   B CA  1 
ATOM   2423 C  C   . GLY   B 1 26  ? 45.943 2.228   11.431  1.00 72.47  ? 719  GLY   B C   1 
ATOM   2424 O  O   . GLY   B 1 26  ? 44.956 2.789   11.902  1.00 72.56  ? 719  GLY   B O   1 
ATOM   2425 N  N   . SER   B 1 27  ? 46.240 2.275   10.129  1.00 72.68  ? 720  SER   B N   1 
ATOM   2426 C  CA  . SER   B 1 27  ? 45.394 2.983   9.173   1.00 73.43  ? 720  SER   B CA  1 
ATOM   2427 C  C   . SER   B 1 27  ? 45.141 2.122   7.948   1.00 74.04  ? 720  SER   B C   1 
ATOM   2428 O  O   . SER   B 1 27  ? 46.038 1.885   7.137   1.00 74.20  ? 720  SER   B O   1 
ATOM   2429 C  CB  . SER   B 1 27  ? 46.008 4.321   8.773   1.00 74.71  ? 720  SER   B CB  1 
ATOM   2430 O  OG  . SER   B 1 27  ? 47.214 4.145   8.049   1.00 77.20  ? 720  SER   B OG  1 
ATOM   2431 N  N   . GLY   B 1 28  ? 43.914 1.647   7.834   1.00 74.16  ? 721  GLY   B N   1 
ATOM   2432 C  CA  . GLY   B 1 28  ? 43.513 0.802   6.728   1.00 74.76  ? 721  GLY   B CA  1 
ATOM   2433 C  C   . GLY   B 1 28  ? 43.047 1.603   5.540   1.00 75.26  ? 721  GLY   B C   1 
ATOM   2434 O  O   . GLY   B 1 28  ? 43.487 2.739   5.324   1.00 75.39  ? 721  GLY   B O   1 
ATOM   2435 N  N   . ALA   B 1 29  ? 42.159 1.003   4.751   1.00 75.27  ? 722  ALA   B N   1 
ATOM   2436 C  CA  . ALA   B 1 29  ? 41.614 1.652   3.565   1.00 75.52  ? 722  ALA   B CA  1 
ATOM   2437 C  C   . ALA   B 1 29  ? 40.417 2.523   3.937   1.00 75.29  ? 722  ALA   B C   1 
ATOM   2438 O  O   . ALA   B 1 29  ? 40.266 3.628   3.420   1.00 75.42  ? 722  ALA   B O   1 
ATOM   2439 C  CB  . ALA   B 1 29  ? 41.197 0.597   2.543   1.00 75.70  ? 722  ALA   B CB  1 
ATOM   2440 N  N   . PHE   B 1 30  ? 39.579 2.026   4.848   1.00 74.69  ? 723  PHE   B N   1 
ATOM   2441 C  CA  . PHE   B 1 30  ? 38.362 2.699   5.263   1.00 74.57  ? 723  PHE   B CA  1 
ATOM   2442 C  C   . PHE   B 1 30  ? 38.565 3.783   6.329   1.00 72.97  ? 723  PHE   B C   1 
ATOM   2443 O  O   . PHE   B 1 30  ? 37.622 4.514   6.603   1.00 73.22  ? 723  PHE   B O   1 
ATOM   2444 C  CB  . PHE   B 1 30  ? 37.327 1.668   5.758   1.00 75.33  ? 723  PHE   B CB  1 
ATOM   2445 C  CG  . PHE   B 1 30  ? 37.136 0.480   4.852   1.00 76.81  ? 723  PHE   B CG  1 
ATOM   2446 C  CD1 . PHE   B 1 30  ? 36.878 0.654   3.504   1.00 77.77  ? 723  PHE   B CD1 1 
ATOM   2447 C  CD2 . PHE   B 1 30  ? 37.230 -0.814  5.347   1.00 78.05  ? 723  PHE   B CD2 1 
ATOM   2448 C  CE1 . PHE   B 1 30  ? 36.722 -0.441  2.667   1.00 78.54  ? 723  PHE   B CE1 1 
ATOM   2449 C  CE2 . PHE   B 1 30  ? 37.063 -1.908  4.511   1.00 78.82  ? 723  PHE   B CE2 1 
ATOM   2450 C  CZ  . PHE   B 1 30  ? 36.808 -1.716  3.177   1.00 78.57  ? 723  PHE   B CZ  1 
ATOM   2451 N  N   . GLY   B 1 31  ? 39.746 3.861   6.944   1.00 71.16  ? 724  GLY   B N   1 
ATOM   2452 C  CA  . GLY   B 1 31  ? 39.995 4.843   7.993   1.00 69.98  ? 724  GLY   B CA  1 
ATOM   2453 C  C   . GLY   B 1 31  ? 41.135 4.499   8.936   1.00 68.48  ? 724  GLY   B C   1 
ATOM   2454 O  O   . GLY   B 1 31  ? 41.963 3.643   8.624   1.00 68.59  ? 724  GLY   B O   1 
ATOM   2455 N  N   . THR   B 1 32  ? 41.202 5.184   10.088  1.00 67.08  ? 725  THR   B N   1 
ATOM   2456 C  CA  . THR   B 1 32  ? 42.288 5.011   11.055  1.00 66.16  ? 725  THR   B CA  1 
ATOM   2457 C  C   . THR   B 1 32  ? 41.777 4.571   12.417  1.00 65.13  ? 725  THR   B C   1 
ATOM   2458 O  O   . THR   B 1 32  ? 40.792 5.131   12.895  1.00 64.96  ? 725  THR   B O   1 
ATOM   2459 C  CB  . THR   B 1 32  ? 43.022 6.356   11.246  1.00 67.17  ? 725  THR   B CB  1 
ATOM   2460 O  OG1 . THR   B 1 32  ? 43.328 6.955   9.982   1.00 67.80  ? 725  THR   B OG1 1 
ATOM   2461 C  CG2 . THR   B 1 32  ? 44.281 6.218   12.087  1.00 67.51  ? 725  THR   B CG2 1 
ATOM   2462 N  N   . VAL   B 1 33  ? 42.459 3.606   13.068  1.00 64.32  ? 726  VAL   B N   1 
ATOM   2463 C  CA  . VAL   B 1 33  ? 42.071 3.194   14.421  1.00 64.28  ? 726  VAL   B CA  1 
ATOM   2464 C  C   . VAL   B 1 33  ? 43.134 3.709   15.415  1.00 64.29  ? 726  VAL   B C   1 
ATOM   2465 O  O   . VAL   B 1 33  ? 44.336 3.636   15.157  1.00 63.98  ? 726  VAL   B O   1 
ATOM   2466 C  CB  . VAL   B 1 33  ? 41.646 1.692   14.650  1.00 64.57  ? 726  VAL   B CB  1 
ATOM   2467 C  CG1 . VAL   B 1 33  ? 41.454 0.928   13.345  1.00 64.98  ? 726  VAL   B CG1 1 
ATOM   2468 C  CG2 . VAL   B 1 33  ? 42.561 0.937   15.616  1.00 64.68  ? 726  VAL   B CG2 1 
ATOM   2469 N  N   . TYR   B 1 34  ? 42.656 4.283   16.520  1.00 64.54  ? 727  TYR   B N   1 
ATOM   2470 C  CA  . TYR   B 1 34  ? 43.477 4.878   17.555  1.00 65.23  ? 727  TYR   B CA  1 
ATOM   2471 C  C   . TYR   B 1 34  ? 43.207 4.236   18.910  1.00 65.39  ? 727  TYR   B C   1 
ATOM   2472 O  O   . TYR   B 1 34  ? 42.071 3.941   19.233  1.00 65.17  ? 727  TYR   B O   1 
ATOM   2473 C  CB  . TYR   B 1 34  ? 43.127 6.374   17.710  1.00 65.62  ? 727  TYR   B CB  1 
ATOM   2474 C  CG  . TYR   B 1 34  ? 43.124 7.212   16.447  1.00 66.77  ? 727  TYR   B CG  1 
ATOM   2475 C  CD1 . TYR   B 1 34  ? 44.275 7.860   16.016  1.00 67.67  ? 727  TYR   B CD1 1 
ATOM   2476 C  CD2 . TYR   B 1 34  ? 41.942 7.471   15.764  1.00 67.60  ? 727  TYR   B CD2 1 
ATOM   2477 C  CE1 . TYR   B 1 34  ? 44.267 8.677   14.890  1.00 68.55  ? 727  TYR   B CE1 1 
ATOM   2478 C  CE2 . TYR   B 1 34  ? 41.921 8.282   14.634  1.00 68.52  ? 727  TYR   B CE2 1 
ATOM   2479 C  CZ  . TYR   B 1 34  ? 43.085 8.895   14.206  1.00 69.41  ? 727  TYR   B CZ  1 
ATOM   2480 O  OH  . TYR   B 1 34  ? 43.070 9.700   13.089  1.00 70.60  ? 727  TYR   B OH  1 
ATOM   2481 N  N   . LYS   B 1 35  ? 44.240 4.112   19.730  1.00 65.72  ? 728  LYS   B N   1 
ATOM   2482 C  CA  . LYS   B 1 35  ? 44.150 3.671   21.113  1.00 66.63  ? 728  LYS   B CA  1 
ATOM   2483 C  C   . LYS   B 1 35  ? 43.739 4.952   21.852  1.00 67.49  ? 728  LYS   B C   1 
ATOM   2484 O  O   . LYS   B 1 35  ? 44.430 5.959   21.723  1.00 68.13  ? 728  LYS   B O   1 
ATOM   2485 C  CB  . LYS   B 1 35  ? 45.549 3.216   21.567  1.00 68.32  ? 728  LYS   B CB  1 
ATOM   2486 C  CG  . LYS   B 1 35  ? 45.745 3.097   23.067  1.00 71.97  ? 728  LYS   B CG  1 
ATOM   2487 C  CD  . LYS   B 1 35  ? 47.169 2.658   23.380  1.00 76.09  ? 728  LYS   B CD  1 
ATOM   2488 C  CE  . LYS   B 1 35  ? 47.419 2.494   24.865  1.00 79.44  ? 728  LYS   B CE  1 
ATOM   2489 N  NZ  . LYS   B 1 35  ? 48.284 1.310   25.159  1.00 81.42  ? 728  LYS   B NZ  1 
ATOM   2490 N  N   . GLY   B 1 36  ? 42.611 4.942   22.551  1.00 67.40  ? 729  GLY   B N   1 
ATOM   2491 C  CA  . GLY   B 1 36  ? 42.132 6.141   23.231  1.00 67.85  ? 729  GLY   B CA  1 
ATOM   2492 C  C   . GLY   B 1 36  ? 41.668 5.961   24.660  1.00 68.32  ? 729  GLY   B C   1 
ATOM   2493 O  O   . GLY   B 1 36  ? 41.821 4.887   25.246  1.00 68.29  ? 729  GLY   B O   1 
ATOM   2494 N  N   . LEU   B 1 37  ? 41.096 7.027   25.230  1.00 68.63  ? 730  LEU   B N   1 
ATOM   2495 C  CA  . LEU   B 1 37  ? 40.588 7.030   26.595  1.00 69.62  ? 730  LEU   B CA  1 
ATOM   2496 C  C   . LEU   B 1 37  ? 39.191 7.635   26.609  1.00 70.60  ? 730  LEU   B C   1 
ATOM   2497 O  O   . LEU   B 1 37  ? 38.946 8.610   25.908  1.00 70.64  ? 730  LEU   B O   1 
ATOM   2498 C  CB  . LEU   B 1 37  ? 41.528 7.840   27.493  1.00 69.89  ? 730  LEU   B CB  1 
ATOM   2499 C  CG  . LEU   B 1 37  ? 41.992 7.143   28.764  1.00 71.39  ? 730  LEU   B CG  1 
ATOM   2500 C  CD1 . LEU   B 1 37  ? 42.782 5.892   28.451  1.00 71.92  ? 730  LEU   B CD1 1 
ATOM   2501 C  CD2 . LEU   B 1 37  ? 42.835 8.062   29.598  1.00 72.08  ? 730  LEU   B CD2 1 
ATOM   2502 N  N   . TRP   B 1 38  ? 38.276 7.068   27.393  1.00 71.53  ? 731  TRP   B N   1 
ATOM   2503 C  CA  . TRP   B 1 38  ? 36.904 7.557   27.428  1.00 73.14  ? 731  TRP   B CA  1 
ATOM   2504 C  C   . TRP   B 1 38  ? 36.341 7.710   28.835  1.00 75.88  ? 731  TRP   B C   1 
ATOM   2505 O  O   . TRP   B 1 38  ? 36.281 6.744   29.590  1.00 75.99  ? 731  TRP   B O   1 
ATOM   2506 C  CB  . TRP   B 1 38  ? 36.012 6.654   26.572  1.00 72.45  ? 731  TRP   B CB  1 
ATOM   2507 C  CG  . TRP   B 1 38  ? 34.539 6.910   26.693  1.00 72.09  ? 731  TRP   B CG  1 
ATOM   2508 C  CD1 . TRP   B 1 38  ? 33.892 8.092   26.498  1.00 72.85  ? 731  TRP   B CD1 1 
ATOM   2509 C  CD2 . TRP   B 1 38  ? 33.522 5.932   26.939  1.00 71.77  ? 731  TRP   B CD2 1 
ATOM   2510 N  NE1 . TRP   B 1 38  ? 32.536 7.921   26.655  1.00 72.98  ? 731  TRP   B NE1 1 
ATOM   2511 C  CE2 . TRP   B 1 38  ? 32.281 6.601   26.916  1.00 72.48  ? 731  TRP   B CE2 1 
ATOM   2512 C  CE3 . TRP   B 1 38  ? 33.538 4.553   27.167  1.00 72.08  ? 731  TRP   B CE3 1 
ATOM   2513 C  CZ2 . TRP   B 1 38  ? 31.070 5.937   27.119  1.00 72.85  ? 731  TRP   B CZ2 1 
ATOM   2514 C  CZ3 . TRP   B 1 38  ? 32.341 3.901   27.386  1.00 72.72  ? 731  TRP   B CZ3 1 
ATOM   2515 C  CH2 . TRP   B 1 38  ? 31.124 4.590   27.359  1.00 72.84  ? 731  TRP   B CH2 1 
ATOM   2516 N  N   . ILE   B 1 39  ? 35.876 8.922   29.158  1.00 77.66  ? 732  ILE   B N   1 
ATOM   2517 C  CA  . ILE   B 1 39  ? 35.249 9.232   30.436  1.00 79.74  ? 732  ILE   B CA  1 
ATOM   2518 C  C   . ILE   B 1 39  ? 33.784 9.505   30.165  1.00 81.47  ? 732  ILE   B C   1 
ATOM   2519 O  O   . ILE   B 1 39  ? 33.436 10.579  29.670  1.00 81.43  ? 732  ILE   B O   1 
ATOM   2520 C  CB  . ILE   B 1 39  ? 35.918 10.458  31.087  1.00 80.80  ? 732  ILE   B CB  1 
ATOM   2521 C  CG1 . ILE   B 1 39  ? 37.437 10.262  31.207  1.00 81.87  ? 732  ILE   B CG1 1 
ATOM   2522 C  CG2 . ILE   B 1 39  ? 35.278 10.776  32.439  1.00 81.59  ? 732  ILE   B CG2 1 
ATOM   2523 C  CD1 . ILE   B 1 39  ? 38.176 11.501  31.581  1.00 83.29  ? 732  ILE   B CD1 1 
ATOM   2524 N  N   . PRO   B 1 40  ? 32.903 8.539   30.456  1.00 82.96  ? 733  PRO   B N   1 
ATOM   2525 C  CA  . PRO   B 1 40  ? 31.471 8.757   30.181  1.00 84.43  ? 733  PRO   B CA  1 
ATOM   2526 C  C   . PRO   B 1 40  ? 30.890 10.003  30.867  1.00 86.49  ? 733  PRO   B C   1 
ATOM   2527 O  O   . PRO   B 1 40  ? 31.487 10.523  31.812  1.00 86.43  ? 733  PRO   B O   1 
ATOM   2528 C  CB  . PRO   B 1 40  ? 30.810 7.447   30.629  1.00 84.79  ? 733  PRO   B CB  1 
ATOM   2529 C  CG  . PRO   B 1 40  ? 31.921 6.442   30.675  1.00 84.75  ? 733  PRO   B CG  1 
ATOM   2530 C  CD  . PRO   B 1 40  ? 33.160 7.204   31.026  1.00 82.71  ? 733  PRO   B CD  1 
ATOM   2531 N  N   . GLU   B 1 41  ? 29.751 10.505  30.355  1.00 88.06  ? 734  GLU   B N   1 
ATOM   2532 C  CA  . GLU   B 1 41  ? 29.091 11.721  30.848  1.00 89.98  ? 734  GLU   B CA  1 
ATOM   2533 C  C   . GLU   B 1 41  ? 28.939 11.777  32.385  1.00 91.41  ? 734  GLU   B C   1 
ATOM   2534 O  O   . GLU   B 1 41  ? 29.504 12.675  33.018  1.00 91.70  ? 734  GLU   B O   1 
ATOM   2535 C  CB  . GLU   B 1 41  ? 27.736 11.956  30.139  1.00 92.60  ? 734  GLU   B CB  1 
ATOM   2536 C  CG  . GLU   B 1 41  ? 27.832 12.791  28.873  1.00 98.23  ? 734  GLU   B CG  1 
ATOM   2537 C  CD  . GLU   B 1 41  ? 27.844 14.300  29.063  1.00 105.50 ? 734  GLU   B CD  1 
ATOM   2538 O  OE1 . GLU   B 1 41  ? 28.892 14.849  29.477  1.00 106.69 ? 734  GLU   B OE1 1 
ATOM   2539 O  OE2 . GLU   B 1 41  ? 26.807 14.940  28.770  1.00 107.99 ? 734  GLU   B OE2 1 
ATOM   2540 N  N   . GLY   B 1 42  ? 28.209 10.826  32.965  1.00 91.96  ? 735  GLY   B N   1 
ATOM   2541 C  CA  . GLY   B 1 42  ? 28.005 10.793  34.406  1.00 92.79  ? 735  GLY   B CA  1 
ATOM   2542 C  C   . GLY   B 1 42  ? 29.255 10.377  35.149  1.00 93.41  ? 735  GLY   B C   1 
ATOM   2543 O  O   . GLY   B 1 42  ? 29.723 11.084  36.045  1.00 93.65  ? 735  GLY   B O   1 
ATOM   2544 N  N   . GLU   B 1 43  ? 29.829 9.245   34.733  1.00 93.44  ? 736  GLU   B N   1 
ATOM   2545 C  CA  . GLU   B 1 43  ? 31.020 8.628   35.311  1.00 93.87  ? 736  GLU   B CA  1 
ATOM   2546 C  C   . GLU   B 1 43  ? 32.212 9.563   35.533  1.00 93.74  ? 736  GLU   B C   1 
ATOM   2547 O  O   . GLU   B 1 43  ? 32.327 10.627  34.918  1.00 93.67  ? 736  GLU   B O   1 
ATOM   2548 C  CB  . GLU   B 1 43  ? 31.454 7.421   34.457  1.00 96.24  ? 736  GLU   B CB  1 
ATOM   2549 C  CG  . GLU   B 1 43  ? 30.655 6.163   34.728  1.00 101.23 ? 736  GLU   B CG  1 
ATOM   2550 C  CD  . GLU   B 1 43  ? 29.408 5.979   33.885  1.00 107.81 ? 736  GLU   B CD  1 
ATOM   2551 O  OE1 . GLU   B 1 43  ? 28.980 4.813   33.728  1.00 109.43 ? 736  GLU   B OE1 1 
ATOM   2552 O  OE2 . GLU   B 1 43  ? 28.850 6.985   33.388  1.00 109.47 ? 736  GLU   B OE2 1 
ATOM   2553 N  N   . LYS   B 1 44  ? 33.085 9.151   36.455  1.00 93.43  ? 737  LYS   B N   1 
ATOM   2554 C  CA  . LYS   B 1 44  ? 34.321 9.850   36.782  1.00 93.50  ? 737  LYS   B CA  1 
ATOM   2555 C  C   . LYS   B 1 44  ? 35.494 8.858   36.669  1.00 93.06  ? 737  LYS   B C   1 
ATOM   2556 O  O   . LYS   B 1 44  ? 36.387 8.855   37.517  1.00 93.34  ? 737  LYS   B O   1 
ATOM   2557 C  CB  . LYS   B 1 44  ? 34.240 10.452  38.195  1.00 95.26  ? 737  LYS   B CB  1 
ATOM   2558 C  CG  . LYS   B 1 44  ? 33.182 11.541  38.322  1.00 99.00  ? 737  LYS   B CG  1 
ATOM   2559 C  CD  . LYS   B 1 44  ? 33.058 12.041  39.747  1.00 103.14 ? 737  LYS   B CD  1 
ATOM   2560 C  CE  . LYS   B 1 44  ? 32.447 13.421  39.800  1.00 106.56 ? 737  LYS   B CE  1 
ATOM   2561 N  NZ  . LYS   B 1 44  ? 33.285 14.424  39.093  1.00 108.38 ? 737  LYS   B NZ  1 
ATOM   2562 N  N   . VAL   B 1 45  ? 35.469 7.998   35.625  1.00 92.02  ? 738  VAL   B N   1 
ATOM   2563 C  CA  . VAL   B 1 45  ? 36.496 6.984   35.358  1.00 91.12  ? 738  VAL   B CA  1 
ATOM   2564 C  C   . VAL   B 1 45  ? 37.005 7.063   33.912  1.00 89.26  ? 738  VAL   B C   1 
ATOM   2565 O  O   . VAL   B 1 45  ? 36.300 7.559   33.036  1.00 89.36  ? 738  VAL   B O   1 
ATOM   2566 C  CB  . VAL   B 1 45  ? 36.012 5.556   35.700  1.00 92.00  ? 738  VAL   B CB  1 
ATOM   2567 C  CG1 . VAL   B 1 45  ? 35.919 5.361   37.210  1.00 92.89  ? 738  VAL   B CG1 1 
ATOM   2568 C  CG2 . VAL   B 1 45  ? 34.682 5.250   35.023  1.00 92.33  ? 738  VAL   B CG2 1 
ATOM   2569 N  N   . LYS   B 1 46  ? 38.225 6.564   33.662  1.00 87.28  ? 739  LYS   B N   1 
ATOM   2570 C  CA  . LYS   B 1 46  ? 38.807 6.597   32.323  1.00 85.63  ? 739  LYS   B CA  1 
ATOM   2571 C  C   . LYS   B 1 46  ? 38.917 5.196   31.722  1.00 83.31  ? 739  LYS   B C   1 
ATOM   2572 O  O   . LYS   B 1 46  ? 39.870 4.470   32.002  1.00 83.49  ? 739  LYS   B O   1 
ATOM   2573 C  CB  . LYS   B 1 46  ? 40.177 7.296   32.332  1.00 87.69  ? 739  LYS   B CB  1 
ATOM   2574 C  CG  . LYS   B 1 46  ? 40.180 8.648   33.055  1.00 92.10  ? 739  LYS   B CG  1 
ATOM   2575 C  CD  . LYS   B 1 46  ? 41.273 9.594   32.544  1.00 96.17  ? 739  LYS   B CD  1 
ATOM   2576 C  CE  . LYS   B 1 46  ? 41.744 10.588  33.585  1.00 99.46  ? 739  LYS   B CE  1 
ATOM   2577 N  NZ  . LYS   B 1 46  ? 40.635 11.427  34.115  1.00 101.41 ? 739  LYS   B NZ  1 
ATOM   2578 N  N   . ILE   B 1 47  ? 37.938 4.821   30.888  1.00 80.87  ? 740  ILE   B N   1 
ATOM   2579 C  CA  . ILE   B 1 47  ? 37.886 3.521   30.222  1.00 78.81  ? 740  ILE   B CA  1 
ATOM   2580 C  C   . ILE   B 1 47  ? 38.807 3.504   28.998  1.00 77.00  ? 740  ILE   B C   1 
ATOM   2581 O  O   . ILE   B 1 47  ? 38.626 4.318   28.092  1.00 77.24  ? 740  ILE   B O   1 
ATOM   2582 C  CB  . ILE   B 1 47  ? 36.432 3.216   29.792  1.00 78.53  ? 740  ILE   B CB  1 
ATOM   2583 C  CG1 . ILE   B 1 47  ? 35.464 3.322   30.976  1.00 79.22  ? 740  ILE   B CG1 1 
ATOM   2584 C  CG2 . ILE   B 1 47  ? 36.339 1.868   29.085  1.00 78.59  ? 740  ILE   B CG2 1 
ATOM   2585 C  CD1 . ILE   B 1 47  ? 34.049 3.368   30.595  1.00 80.49  ? 740  ILE   B CD1 1 
ATOM   2586 N  N   . PRO   B 1 48  ? 39.772 2.564   28.925  1.00 74.75  ? 741  PRO   B N   1 
ATOM   2587 C  CA  . PRO   B 1 48  ? 40.635 2.503   27.733  1.00 72.95  ? 741  PRO   B CA  1 
ATOM   2588 C  C   . PRO   B 1 48  ? 39.903 1.893   26.542  1.00 70.65  ? 741  PRO   B C   1 
ATOM   2589 O  O   . PRO   B 1 48  ? 39.510 0.729   26.588  1.00 71.05  ? 741  PRO   B O   1 
ATOM   2590 C  CB  . PRO   B 1 48  ? 41.831 1.663   28.183  1.00 73.93  ? 741  PRO   B CB  1 
ATOM   2591 C  CG  . PRO   B 1 48  ? 41.396 0.958   29.413  1.00 74.86  ? 741  PRO   B CG  1 
ATOM   2592 C  CD  . PRO   B 1 48  ? 40.103 1.517   29.911  1.00 73.82  ? 741  PRO   B CD  1 
ATOM   2593 N  N   . VAL   B 1 49  ? 39.678 2.700   25.492  1.00 68.00  ? 742  VAL   B N   1 
ATOM   2594 C  CA  . VAL   B 1 49  ? 38.935 2.285   24.302  1.00 65.67  ? 742  VAL   B CA  1 
ATOM   2595 C  C   . VAL   B 1 49  ? 39.803 2.286   23.010  1.00 63.05  ? 742  VAL   B C   1 
ATOM   2596 O  O   . VAL   B 1 49  ? 40.983 2.618   23.047  1.00 63.23  ? 742  VAL   B O   1 
ATOM   2597 C  CB  . VAL   B 1 49  ? 37.660 3.172   24.149  1.00 66.02  ? 742  VAL   B CB  1 
ATOM   2598 C  CG1 . VAL   B 1 49  ? 36.781 3.110   25.390  1.00 66.52  ? 742  VAL   B CG1 1 
ATOM   2599 C  CG2 . VAL   B 1 49  ? 38.031 4.603   23.798  1.00 66.41  ? 742  VAL   B CG2 1 
ATOM   2600 N  N   . ALA   B 1 50  ? 39.223 1.850   21.890  1.00 60.39  ? 743  ALA   B N   1 
ATOM   2601 C  CA  . ALA   B 1 50  ? 39.805 1.902   20.567  1.00 58.28  ? 743  ALA   B CA  1 
ATOM   2602 C  C   . ALA   B 1 50  ? 38.795 2.677   19.716  1.00 55.76  ? 743  ALA   B C   1 
ATOM   2603 O  O   . ALA   B 1 50  ? 37.593 2.413   19.777  1.00 55.44  ? 743  ALA   B O   1 
ATOM   2604 C  CB  . ALA   B 1 50  ? 39.993 0.513   20.019  1.00 58.50  ? 743  ALA   B CB  1 
ATOM   2605 N  N   . ILE   B 1 51  ? 39.265 3.699   19.007  1.00 53.95  ? 744  ILE   B N   1 
ATOM   2606 C  CA  . ILE   B 1 51  ? 38.397 4.553   18.209  1.00 52.65  ? 744  ILE   B CA  1 
ATOM   2607 C  C   . ILE   B 1 51  ? 38.686 4.370   16.739  1.00 51.23  ? 744  ILE   B C   1 
ATOM   2608 O  O   . ILE   B 1 51  ? 39.818 4.551   16.320  1.00 51.35  ? 744  ILE   B O   1 
ATOM   2609 C  CB  . ILE   B 1 51  ? 38.597 6.023   18.621  1.00 53.06  ? 744  ILE   B CB  1 
ATOM   2610 C  CG1 . ILE   B 1 51  ? 38.370 6.212   20.124  1.00 53.89  ? 744  ILE   B CG1 1 
ATOM   2611 C  CG2 . ILE   B 1 51  ? 37.719 6.957   17.792  1.00 53.48  ? 744  ILE   B CG2 1 
ATOM   2612 C  CD1 . ILE   B 1 51  ? 39.462 6.968   20.785  1.00 55.16  ? 744  ILE   B CD1 1 
ATOM   2613 N  N   . LYS   B 1 52  ? 37.676 4.005   15.952  1.00 50.00  ? 745  LYS   B N   1 
ATOM   2614 C  CA  . LYS   B 1 52  ? 37.847 3.848   14.517  1.00 49.42  ? 745  LYS   B CA  1 
ATOM   2615 C  C   . LYS   B 1 52  ? 37.208 5.047   13.852  1.00 48.71  ? 745  LYS   B C   1 
ATOM   2616 O  O   . LYS   B 1 52  ? 36.003 5.242   13.959  1.00 48.16  ? 745  LYS   B O   1 
ATOM   2617 C  CB  . LYS   B 1 52  ? 37.223 2.542   14.000  1.00 50.85  ? 745  LYS   B CB  1 
ATOM   2618 C  CG  . LYS   B 1 52  ? 37.320 2.412   12.481  1.00 53.71  ? 745  LYS   B CG  1 
ATOM   2619 C  CD  . LYS   B 1 52  ? 37.858 1.059   12.062  1.00 56.20  ? 745  LYS   B CD  1 
ATOM   2620 C  CE  . LYS   B 1 52  ? 36.791 0.004   12.041  1.00 58.90  ? 745  LYS   B CE  1 
ATOM   2621 N  NZ  . LYS   B 1 52  ? 37.377 -1.339  11.791  1.00 61.12  ? 745  LYS   B NZ  1 
ATOM   2622 N  N   . GLU   B 1 53  ? 38.026 5.887   13.220  1.00 48.35  ? 746  GLU   B N   1 
ATOM   2623 C  CA  . GLU   B 1 53  ? 37.519 7.055   12.524  1.00 48.33  ? 746  GLU   B CA  1 
ATOM   2624 C  C   . GLU   B 1 53  ? 37.491 6.717   11.052  1.00 48.32  ? 746  GLU   B C   1 
ATOM   2625 O  O   . GLU   B 1 53  ? 38.548 6.575   10.423  1.00 48.25  ? 746  GLU   B O   1 
ATOM   2626 C  CB  . GLU   B 1 53  ? 38.393 8.286   12.769  1.00 50.08  ? 746  GLU   B CB  1 
ATOM   2627 C  CG  . GLU   B 1 53  ? 37.720 9.562   12.278  1.00 53.11  ? 746  GLU   B CG  1 
ATOM   2628 C  CD  . GLU   B 1 53  ? 38.437 10.846  12.622  1.00 57.59  ? 746  GLU   B CD  1 
ATOM   2629 O  OE1 . GLU   B 1 53  ? 39.689 10.841  12.621  1.00 58.89  ? 746  GLU   B OE1 1 
ATOM   2630 O  OE2 . GLU   B 1 53  ? 37.750 11.858  12.890  1.00 58.85  ? 746  GLU   B OE2 1 
ATOM   2631 N  N   . LEU   B 1 54  ? 36.285 6.513   10.520  1.00 47.90  ? 747  LEU   B N   1 
ATOM   2632 C  CA  . LEU   B 1 54  ? 36.140 6.188   9.113   1.00 48.20  ? 747  LEU   B CA  1 
ATOM   2633 C  C   . LEU   B 1 54  ? 36.489 7.435   8.277   1.00 49.12  ? 747  LEU   B C   1 
ATOM   2634 O  O   . LEU   B 1 54  ? 36.125 8.562   8.652   1.00 49.16  ? 747  LEU   B O   1 
ATOM   2635 C  CB  . LEU   B 1 54  ? 34.706 5.734   8.821   1.00 48.00  ? 747  LEU   B CB  1 
ATOM   2636 C  CG  . LEU   B 1 54  ? 34.178 4.548   9.632   1.00 48.76  ? 747  LEU   B CG  1 
ATOM   2637 C  CD1 . LEU   B 1 54  ? 32.714 4.285   9.320   1.00 48.80  ? 747  LEU   B CD1 1 
ATOM   2638 C  CD2 . LEU   B 1 54  ? 35.025 3.298   9.406   1.00 49.25  ? 747  LEU   B CD2 1 
ATOM   2639 N  N   . ARG   B 1 55  ? 37.226 7.251   7.142   1.00 49.21  ? 748  ARG   B N   1 
ATOM   2640 C  CA  . ARG   B 1 55  ? 37.603 8.365   6.253   1.00 49.27  ? 748  ARG   B CA  1 
ATOM   2641 C  C   . ARG   B 1 55  ? 36.356 9.136   5.819   1.00 48.78  ? 748  ARG   B C   1 
ATOM   2642 O  O   . ARG   B 1 55  ? 35.300 8.538   5.634   1.00 48.70  ? 748  ARG   B O   1 
ATOM   2643 C  CB  . ARG   B 1 55  ? 38.497 7.903   5.074   1.00 51.36  ? 748  ARG   B CB  1 
ATOM   2644 C  CG  . ARG   B 1 55  ? 37.950 8.127   3.646   1.00 56.27  ? 748  ARG   B CG  1 
ATOM   2645 C  CD  . ARG   B 1 55  ? 38.824 9.054   2.801   1.00 60.19  ? 748  ARG   B CD  1 
ATOM   2646 N  NE  . ARG   B 1 55  ? 38.202 9.401   1.517   1.00 63.42  ? 748  ARG   B NE  1 
ATOM   2647 C  CZ  . ARG   B 1 55  ? 38.751 10.215  0.616   1.00 66.44  ? 748  ARG   B CZ  1 
ATOM   2648 N  NH1 . ARG   B 1 55  ? 38.122 10.476  -0.522  1.00 65.54  ? 748  ARG   B NH1 1 
ATOM   2649 N  NH2 . ARG   B 1 55  ? 39.938 10.773  0.848   1.00 66.71  ? 748  ARG   B NH2 1 
ATOM   2650 N  N   . GLU   B 1 56  ? 36.441 10.459  5.804   1.00 48.40  ? 749  GLU   B N   1 
ATOM   2651 C  CA  . GLU   B 1 56  ? 35.284 11.292  5.514   1.00 48.15  ? 749  GLU   B CA  1 
ATOM   2652 C  C   . GLU   B 1 56  ? 34.680 11.011  4.149   1.00 48.55  ? 749  GLU   B C   1 
ATOM   2653 O  O   . GLU   B 1 56  ? 35.400 10.632  3.223   1.00 48.92  ? 749  GLU   B O   1 
ATOM   2654 C  CB  . GLU   B 1 56  ? 35.649 12.759  5.663   1.00 49.18  ? 749  GLU   B CB  1 
ATOM   2655 C  CG  . GLU   B 1 56  ? 34.440 13.652  5.835   1.00 51.19  ? 749  GLU   B CG  1 
ATOM   2656 C  CD  . GLU   B 1 56  ? 34.755 15.127  5.918   1.00 53.28  ? 749  GLU   B CD  1 
ATOM   2657 O  OE1 . GLU   B 1 56  ? 35.903 15.474  6.276   1.00 53.87  ? 749  GLU   B OE1 1 
ATOM   2658 O  OE2 . GLU   B 1 56  ? 33.856 15.940  5.611   1.00 53.98  ? 749  GLU   B OE2 1 
ATOM   2659 N  N   . ALA   B 1 57  ? 33.353 11.182  4.036   1.00 48.66  ? 750  ALA   B N   1 
ATOM   2660 C  CA  . ALA   B 1 57  ? 32.567 10.985  2.816   1.00 49.49  ? 750  ALA   B CA  1 
ATOM   2661 C  C   . ALA   B 1 57  ? 32.751 9.604   2.221   1.00 50.83  ? 750  ALA   B C   1 
ATOM   2662 O  O   . ALA   B 1 57  ? 32.801 9.430   1.002   1.00 51.31  ? 750  ALA   B O   1 
ATOM   2663 C  CB  . ALA   B 1 57  ? 32.853 12.068  1.786   1.00 49.43  ? 750  ALA   B CB  1 
ATOM   2664 N  N   . THR   B 1 58  ? 32.803 8.608   3.099   1.00 51.27  ? 751  THR   B N   1 
ATOM   2665 C  CA  . THR   B 1 58  ? 32.975 7.215   2.728   1.00 51.82  ? 751  THR   B CA  1 
ATOM   2666 C  C   . THR   B 1 58  ? 31.610 6.482   2.700   1.00 53.01  ? 751  THR   B C   1 
ATOM   2667 O  O   . THR   B 1 58  ? 31.458 5.512   1.971   1.00 53.34  ? 751  THR   B O   1 
ATOM   2668 C  CB  . THR   B 1 58  ? 34.054 6.630   3.653   1.00 52.48  ? 751  THR   B CB  1 
ATOM   2669 O  OG1 . THR   B 1 58  ? 35.178 6.203   2.887   1.00 53.10  ? 751  THR   B OG1 1 
ATOM   2670 C  CG2 . THR   B 1 58  ? 33.559 5.553   4.601   1.00 52.85  ? 751  THR   B CG2 1 
ATOM   2671 N  N   . SER   B 1 59  ? 30.623 6.952   3.463   1.00 53.90  ? 752  SER   B N   1 
ATOM   2672 C  CA  . SER   B 1 59  ? 29.309 6.327   3.509   1.00 55.41  ? 752  SER   B CA  1 
ATOM   2673 C  C   . SER   B 1 59  ? 28.254 7.113   2.729   1.00 56.78  ? 752  SER   B C   1 
ATOM   2674 O  O   . SER   B 1 59  ? 28.075 8.315   2.934   1.00 56.90  ? 752  SER   B O   1 
ATOM   2675 C  CB  . SER   B 1 59  ? 28.848 6.145   4.955   1.00 56.91  ? 752  SER   B CB  1 
ATOM   2676 O  OG  . SER   B 1 59  ? 27.621 5.437   4.979   1.00 59.44  ? 752  SER   B OG  1 
ATOM   2677 N  N   . PRO   B 1 60  ? 27.447 6.411   1.923   1.00 57.56  ? 753  PRO   B N   1 
ATOM   2678 C  CA  . PRO   B 1 60  ? 26.392 7.092   1.162   1.00 58.36  ? 753  PRO   B CA  1 
ATOM   2679 C  C   . PRO   B 1 60  ? 25.097 7.295   1.940   1.00 59.98  ? 753  PRO   B C   1 
ATOM   2680 O  O   . PRO   B 1 60  ? 24.030 7.288   1.329   1.00 60.60  ? 753  PRO   B O   1 
ATOM   2681 C  CB  . PRO   B 1 60  ? 26.143 6.118   0.015   1.00 58.78  ? 753  PRO   B CB  1 
ATOM   2682 C  CG  . PRO   B 1 60  ? 26.372 4.811   0.610   1.00 59.01  ? 753  PRO   B CG  1 
ATOM   2683 C  CD  . PRO   B 1 60  ? 27.518 4.982   1.573   1.00 57.21  ? 753  PRO   B CD  1 
ATOM   2684 N  N   . LYS   B 1 61  ? 25.173 7.418   3.277   1.00 60.46  ? 754  LYS   B N   1 
ATOM   2685 C  CA  . LYS   B 1 61  ? 23.990 7.554   4.112   1.00 61.39  ? 754  LYS   B CA  1 
ATOM   2686 C  C   . LYS   B 1 61  ? 24.034 8.806   4.948   1.00 63.02  ? 754  LYS   B C   1 
ATOM   2687 O  O   . LYS   B 1 61  ? 25.102 9.195   5.423   1.00 62.88  ? 754  LYS   B O   1 
ATOM   2688 C  CB  . LYS   B 1 61  ? 23.869 6.341   5.037   1.00 62.52  ? 754  LYS   B CB  1 
ATOM   2689 C  CG  . LYS   B 1 61  ? 23.641 5.050   4.292   1.00 65.59  ? 754  LYS   B CG  1 
ATOM   2690 C  CD  . LYS   B 1 61  ? 24.184 3.859   5.034   1.00 68.73  ? 754  LYS   B CD  1 
ATOM   2691 C  CE  . LYS   B 1 61  ? 23.704 2.587   4.393   1.00 71.63  ? 754  LYS   B CE  1 
ATOM   2692 N  NZ  . LYS   B 1 61  ? 22.236 2.422   4.574   1.00 73.83  ? 754  LYS   B NZ  1 
ATOM   2693 N  N   . ALA   B 1 62  ? 22.865 9.422   5.163   1.00 64.42  ? 755  ALA   B N   1 
ATOM   2694 C  CA  . ALA   B 1 62  ? 22.768 10.605  6.012   1.00 66.34  ? 755  ALA   B CA  1 
ATOM   2695 C  C   . ALA   B 1 62  ? 22.957 10.200  7.493   1.00 67.84  ? 755  ALA   B C   1 
ATOM   2696 O  O   . ALA   B 1 62  ? 22.785 9.028   7.842   1.00 67.98  ? 755  ALA   B O   1 
ATOM   2697 C  CB  . ALA   B 1 62  ? 21.419 11.281  5.816   1.00 66.75  ? 755  ALA   B CB  1 
ATOM   2698 N  N   . ASN   B 1 63  ? 23.301 11.161  8.361   1.00 68.59  ? 756  ASN   B N   1 
ATOM   2699 C  CA  . ASN   B 1 63  ? 23.556 10.874  9.770   1.00 70.05  ? 756  ASN   B CA  1 
ATOM   2700 C  C   . ASN   B 1 63  ? 22.419 10.114  10.498  1.00 71.34  ? 756  ASN   B C   1 
ATOM   2701 O  O   . ASN   B 1 63  ? 22.701 9.388   11.456  1.00 71.62  ? 756  ASN   B O   1 
ATOM   2702 C  CB  . ASN   B 1 63  ? 23.945 12.142  10.523  1.00 71.38  ? 756  ASN   B CB  1 
ATOM   2703 C  CG  . ASN   B 1 63  ? 25.415 12.518  10.403  1.00 74.60  ? 756  ASN   B CG  1 
ATOM   2704 O  OD1 . ASN   B 1 63  ? 25.913 13.391  11.116  1.00 76.10  ? 756  ASN   B OD1 1 
ATOM   2705 N  ND2 . ASN   B 1 63  ? 26.157 11.880  9.508   1.00 74.94  ? 756  ASN   B ND2 1 
ATOM   2706 N  N   . LYS   B 1 64  ? 21.167 10.221  10.021  1.00 71.70  ? 757  LYS   B N   1 
ATOM   2707 C  CA  . LYS   B 1 64  ? 20.070 9.490   10.638  1.00 72.37  ? 757  LYS   B CA  1 
ATOM   2708 C  C   . LYS   B 1 64  ? 20.123 8.028   10.239  1.00 72.93  ? 757  LYS   B C   1 
ATOM   2709 O  O   . LYS   B 1 64  ? 19.923 7.169   11.090  1.00 73.65  ? 757  LYS   B O   1 
ATOM   2710 C  CB  . LYS   B 1 64  ? 18.715 10.123  10.314  1.00 74.70  ? 757  LYS   B CB  1 
ATOM   2711 C  CG  . LYS   B 1 64  ? 18.570 11.568  10.822  1.00 79.83  ? 757  LYS   B CG  1 
ATOM   2712 C  CD  . LYS   B 1 64  ? 18.370 11.685  12.351  1.00 84.52  ? 757  LYS   B CD  1 
ATOM   2713 C  CE  . LYS   B 1 64  ? 19.599 12.153  13.112  1.00 88.14  ? 757  LYS   B CE  1 
ATOM   2714 N  NZ  . LYS   B 1 64  ? 20.298 13.268  12.421  1.00 90.26  ? 757  LYS   B NZ  1 
ATOM   2715 N  N   . GLU   B 1 65  ? 20.440 7.730   8.970   1.00 72.52  ? 758  GLU   B N   1 
ATOM   2716 C  CA  . GLU   B 1 65  ? 20.542 6.338   8.519   1.00 72.52  ? 758  GLU   B CA  1 
ATOM   2717 C  C   . GLU   B 1 65  ? 21.775 5.635   9.059   1.00 72.24  ? 758  GLU   B C   1 
ATOM   2718 O  O   . GLU   B 1 65  ? 21.748 4.415   9.218   1.00 72.32  ? 758  GLU   B O   1 
ATOM   2719 C  CB  . GLU   B 1 65  ? 20.480 6.221   6.998   1.00 75.08  ? 758  GLU   B CB  1 
ATOM   2720 C  CG  . GLU   B 1 65  ? 19.090 6.468   6.449   1.00 80.72  ? 758  GLU   B CG  1 
ATOM   2721 C  CD  . GLU   B 1 65  ? 18.812 7.925   6.139   1.00 87.86  ? 758  GLU   B CD  1 
ATOM   2722 O  OE1 . GLU   B 1 65  ? 17.982 8.540   6.848   1.00 89.85  ? 758  GLU   B OE1 1 
ATOM   2723 O  OE2 . GLU   B 1 65  ? 19.438 8.457   5.192   1.00 89.53  ? 758  GLU   B OE2 1 
ATOM   2724 N  N   . ILE   B 1 66  ? 22.853 6.393   9.356   1.00 71.70  ? 759  ILE   B N   1 
ATOM   2725 C  CA  . ILE   B 1 66  ? 24.069 5.844   9.961   1.00 71.42  ? 759  ILE   B CA  1 
ATOM   2726 C  C   . ILE   B 1 66  ? 23.707 5.374   11.371  1.00 72.12  ? 759  ILE   B C   1 
ATOM   2727 O  O   . ILE   B 1 66  ? 23.975 4.229   11.719  1.00 72.34  ? 759  ILE   B O   1 
ATOM   2728 C  CB  . ILE   B 1 66  ? 25.213 6.888   9.968   1.00 70.90  ? 759  ILE   B CB  1 
ATOM   2729 C  CG1 . ILE   B 1 66  ? 25.770 7.085   8.547   1.00 71.14  ? 759  ILE   B CG1 1 
ATOM   2730 C  CG2 . ILE   B 1 66  ? 26.322 6.514   10.955  1.00 71.20  ? 759  ILE   B CG2 1 
ATOM   2731 C  CD1 . ILE   B 1 66  ? 26.653 8.240   8.404   1.00 72.00  ? 759  ILE   B CD1 1 
ATOM   2732 N  N   . LEU   B 1 67  ? 23.017 6.231   12.136  1.00 72.43  ? 760  LEU   B N   1 
ATOM   2733 C  CA  . LEU   B 1 67  ? 22.546 5.944   13.487  1.00 73.20  ? 760  LEU   B CA  1 
ATOM   2734 C  C   . LEU   B 1 67  ? 21.601 4.731   13.532  1.00 73.55  ? 760  LEU   B C   1 
ATOM   2735 O  O   . LEU   B 1 67  ? 21.671 3.946   14.475  1.00 73.51  ? 760  LEU   B O   1 
ATOM   2736 C  CB  . LEU   B 1 67  ? 21.865 7.198   14.071  1.00 73.62  ? 760  LEU   B CB  1 
ATOM   2737 C  CG  . LEU   B 1 67  ? 22.597 8.062   15.137  1.00 75.88  ? 760  LEU   B CG  1 
ATOM   2738 C  CD1 . LEU   B 1 67  ? 24.083 7.695   15.346  1.00 76.76  ? 760  LEU   B CD1 1 
ATOM   2739 C  CD2 . LEU   B 1 67  ? 22.453 9.534   14.828  1.00 76.80  ? 760  LEU   B CD2 1 
ATOM   2740 N  N   . ASP   B 1 68  ? 20.776 4.539   12.490  1.00 73.53  ? 761  ASP   B N   1 
ATOM   2741 C  CA  . ASP   B 1 68  ? 19.861 3.402   12.388  1.00 73.96  ? 761  ASP   B CA  1 
ATOM   2742 C  C   . ASP   B 1 68  ? 20.657 2.099   12.311  1.00 73.62  ? 761  ASP   B C   1 
ATOM   2743 O  O   . ASP   B 1 68  ? 20.306 1.129   12.980  1.00 73.88  ? 761  ASP   B O   1 
ATOM   2744 C  CB  . ASP   B 1 68  ? 18.933 3.544   11.164  1.00 76.36  ? 761  ASP   B CB  1 
ATOM   2745 C  CG  . ASP   B 1 68  ? 17.869 4.624   11.299  1.00 82.30  ? 761  ASP   B CG  1 
ATOM   2746 O  OD1 . ASP   B 1 68  ? 17.673 5.134   12.433  1.00 83.52  ? 761  ASP   B OD1 1 
ATOM   2747 O  OD2 . ASP   B 1 68  ? 17.244 4.977   10.268  1.00 84.35  ? 761  ASP   B OD2 1 
ATOM   2748 N  N   . GLU   B 1 69  ? 21.746 2.078   11.531  1.00 72.90  ? 762  GLU   B N   1 
ATOM   2749 C  CA  . GLU   B 1 69  ? 22.600 0.887   11.449  1.00 72.62  ? 762  GLU   B CA  1 
ATOM   2750 C  C   . GLU   B 1 69  ? 23.558 0.744   12.632  1.00 71.72  ? 762  GLU   B C   1 
ATOM   2751 O  O   . GLU   B 1 69  ? 24.084 -0.347  12.859  1.00 71.87  ? 762  GLU   B O   1 
ATOM   2752 C  CB  . GLU   B 1 69  ? 23.372 0.842   10.142  1.00 74.95  ? 762  GLU   B CB  1 
ATOM   2753 C  CG  . GLU   B 1 69  ? 22.557 0.269   9.004   1.00 80.55  ? 762  GLU   B CG  1 
ATOM   2754 C  CD  . GLU   B 1 69  ? 23.158 0.552   7.646   1.00 88.19  ? 762  GLU   B CD  1 
ATOM   2755 O  OE1 . GLU   B 1 69  ? 22.918 -0.241  6.709   1.00 89.35  ? 762  GLU   B OE1 1 
ATOM   2756 O  OE2 . GLU   B 1 69  ? 23.871 1.573   7.520   1.00 91.48  ? 762  GLU   B OE2 1 
ATOM   2757 N  N   . ALA   B 1 70  ? 23.790 1.838   13.372  1.00 70.44  ? 763  ALA   B N   1 
ATOM   2758 C  CA  . ALA   B 1 70  ? 24.598 1.840   14.576  1.00 69.74  ? 763  ALA   B CA  1 
ATOM   2759 C  C   . ALA   B 1 70  ? 23.783 1.188   15.705  1.00 69.03  ? 763  ALA   B C   1 
ATOM   2760 O  O   . ALA   B 1 70  ? 24.352 0.433   16.489  1.00 69.01  ? 763  ALA   B O   1 
ATOM   2761 C  CB  . ALA   B 1 70  ? 24.989 3.259   14.939  1.00 69.79  ? 763  ALA   B CB  1 
ATOM   2762 N  N   . TYR   B 1 71  ? 22.445 1.437   15.762  1.00 68.42  ? 764  TYR   B N   1 
ATOM   2763 C  CA  . TYR   B 1 71  ? 21.551 0.779   16.727  1.00 68.23  ? 764  TYR   B CA  1 
ATOM   2764 C  C   . TYR   B 1 71  ? 21.457 -0.734  16.435  1.00 67.54  ? 764  TYR   B C   1 
ATOM   2765 O  O   . TYR   B 1 71  ? 21.254 -1.518  17.352  1.00 68.28  ? 764  TYR   B O   1 
ATOM   2766 C  CB  . TYR   B 1 71  ? 20.158 1.444   16.785  1.00 68.70  ? 764  TYR   B CB  1 
ATOM   2767 C  CG  . TYR   B 1 71  ? 20.208 2.805   17.452  1.00 70.43  ? 764  TYR   B CG  1 
ATOM   2768 C  CD1 . TYR   B 1 71  ? 20.863 2.984   18.661  1.00 71.58  ? 764  TYR   B CD1 1 
ATOM   2769 C  CD2 . TYR   B 1 71  ? 19.617 3.916   16.863  1.00 71.61  ? 764  TYR   B CD2 1 
ATOM   2770 C  CE1 . TYR   B 1 71  ? 20.952 4.236   19.258  1.00 72.53  ? 764  TYR   B CE1 1 
ATOM   2771 C  CE2 . TYR   B 1 71  ? 19.713 5.177   17.442  1.00 72.51  ? 764  TYR   B CE2 1 
ATOM   2772 C  CZ  . TYR   B 1 71  ? 20.380 5.334   18.645  1.00 73.53  ? 764  TYR   B CZ  1 
ATOM   2773 O  OH  . TYR   B 1 71  ? 20.476 6.573   19.245  1.00 75.13  ? 764  TYR   B OH  1 
ATOM   2774 N  N   . VAL   B 1 72  ? 21.656 -1.144  15.178  1.00 65.92  ? 765  VAL   B N   1 
ATOM   2775 C  CA  . VAL   B 1 72  ? 21.682 -2.535  14.778  1.00 64.83  ? 765  VAL   B CA  1 
ATOM   2776 C  C   . VAL   B 1 72  ? 22.942 -3.218  15.344  1.00 63.96  ? 765  VAL   B C   1 
ATOM   2777 O  O   . VAL   B 1 72  ? 22.795 -4.179  16.108  1.00 64.11  ? 765  VAL   B O   1 
ATOM   2778 C  CB  . VAL   B 1 72  ? 21.557 -2.660  13.248  1.00 65.15  ? 765  VAL   B CB  1 
ATOM   2779 C  CG1 . VAL   B 1 72  ? 21.932 -4.056  12.772  1.00 65.67  ? 765  VAL   B CG1 1 
ATOM   2780 C  CG2 . VAL   B 1 72  ? 20.151 -2.288  12.798  1.00 65.29  ? 765  VAL   B CG2 1 
ATOM   2781 N  N   . MET   B 1 73  ? 24.164 -2.691  15.070  1.00 62.79  ? 766  MET   B N   1 
ATOM   2782 C  CA  . MET   B 1 73  ? 25.382 -3.292  15.657  1.00 62.26  ? 766  MET   B CA  1 
ATOM   2783 C  C   . MET   B 1 73  ? 25.449 -3.186  17.213  1.00 61.42  ? 766  MET   B C   1 
ATOM   2784 O  O   . MET   B 1 73  ? 26.304 -3.810  17.851  1.00 61.48  ? 766  MET   B O   1 
ATOM   2785 C  CB  . MET   B 1 73  ? 26.700 -2.810  15.016  1.00 62.77  ? 766  MET   B CB  1 
ATOM   2786 C  CG  . MET   B 1 73  ? 26.665 -1.445  14.396  1.00 64.93  ? 766  MET   B CG  1 
ATOM   2787 S  SD  . MET   B 1 73  ? 28.128 -1.194  13.358  1.00 67.81  ? 766  MET   B SD  1 
ATOM   2788 C  CE  . MET   B 1 73  ? 27.586 0.155   12.414  1.00 66.25  ? 766  MET   B CE  1 
ATOM   2789 N  N   . ALA   B 1 74  ? 24.525 -2.432  17.815  1.00 60.25  ? 767  ALA   B N   1 
ATOM   2790 C  CA  . ALA   B 1 74  ? 24.408 -2.362  19.262  1.00 59.61  ? 767  ALA   B CA  1 
ATOM   2791 C  C   . ALA   B 1 74  ? 23.307 -3.353  19.758  1.00 58.71  ? 767  ALA   B C   1 
ATOM   2792 O  O   . ALA   B 1 74  ? 23.373 -3.824  20.890  1.00 59.21  ? 767  ALA   B O   1 
ATOM   2793 C  CB  . ALA   B 1 74  ? 24.083 -0.950  19.693  1.00 59.66  ? 767  ALA   B CB  1 
ATOM   2794 N  N   . SER   B 1 75  ? 22.317 -3.683  18.915  1.00 57.15  ? 768  SER   B N   1 
ATOM   2795 C  CA  . SER   B 1 75  ? 21.278 -4.632  19.279  1.00 56.32  ? 768  SER   B CA  1 
ATOM   2796 C  C   . SER   B 1 75  ? 21.834 -6.058  19.410  1.00 54.74  ? 768  SER   B C   1 
ATOM   2797 O  O   . SER   B 1 75  ? 21.238 -6.863  20.116  1.00 54.80  ? 768  SER   B O   1 
ATOM   2798 C  CB  . SER   B 1 75  ? 20.147 -4.601  18.260  1.00 58.35  ? 768  SER   B CB  1 
ATOM   2799 O  OG  . SER   B 1 75  ? 20.601 -5.056  16.997  1.00 61.73  ? 768  SER   B OG  1 
ATOM   2800 N  N   . VAL   B 1 76  ? 22.966 -6.380  18.745  1.00 53.27  ? 769  VAL   B N   1 
ATOM   2801 C  CA  . VAL   B 1 76  ? 23.551 -7.721  18.856  1.00 52.15  ? 769  VAL   B CA  1 
ATOM   2802 C  C   . VAL   B 1 76  ? 24.116 -7.998  20.244  1.00 50.94  ? 769  VAL   B C   1 
ATOM   2803 O  O   . VAL   B 1 76  ? 24.453 -9.143  20.521  1.00 50.88  ? 769  VAL   B O   1 
ATOM   2804 C  CB  . VAL   B 1 76  ? 24.579 -8.075  17.755  1.00 52.55  ? 769  VAL   B CB  1 
ATOM   2805 C  CG1 . VAL   B 1 76  ? 24.064 -7.682  16.380  1.00 52.97  ? 769  VAL   B CG1 1 
ATOM   2806 C  CG2 . VAL   B 1 76  ? 25.930 -7.436  18.037  1.00 52.93  ? 769  VAL   B CG2 1 
ATOM   2807 N  N   . ASP   B 1 77  ? 24.197 -6.982  21.127  1.00 49.85  ? 770  ASP   B N   1 
ATOM   2808 C  CA  . ASP   B 1 77  ? 24.647 -7.171  22.503  1.00 49.41  ? 770  ASP   B CA  1 
ATOM   2809 C  C   . ASP   B 1 77  ? 23.557 -7.874  23.357  1.00 48.32  ? 770  ASP   B C   1 
ATOM   2810 O  O   . ASP   B 1 77  ? 23.801 -8.142  24.531  1.00 48.65  ? 770  ASP   B O   1 
ATOM   2811 C  CB  . ASP   B 1 77  ? 25.002 -5.827  23.151  1.00 52.24  ? 770  ASP   B CB  1 
ATOM   2812 C  CG  . ASP   B 1 77  ? 25.700 -4.804  22.263  1.00 60.21  ? 770  ASP   B CG  1 
ATOM   2813 O  OD1 . ASP   B 1 77  ? 26.375 -5.216  21.292  1.00 62.25  ? 770  ASP   B OD1 1 
ATOM   2814 O  OD2 . ASP   B 1 77  ? 25.578 -3.585  22.546  1.00 63.42  ? 770  ASP   B OD2 1 
ATOM   2815 N  N   . ASN   B 1 78  ? 22.374 -8.191  22.776  1.00 46.98  ? 771  ASN   B N   1 
ATOM   2816 C  CA  . ASN   B 1 78  ? 21.261 -8.852  23.441  1.00 46.38  ? 771  ASN   B CA  1 
ATOM   2817 C  C   . ASN   B 1 78  ? 20.780 -10.060 22.622  1.00 45.22  ? 771  ASN   B C   1 
ATOM   2818 O  O   . ASN   B 1 78  ? 20.240 -9.890  21.528  1.00 45.51  ? 771  ASN   B O   1 
ATOM   2819 C  CB  . ASN   B 1 78  ? 20.125 -7.862  23.664  1.00 47.78  ? 771  ASN   B CB  1 
ATOM   2820 C  CG  . ASN   B 1 78  ? 19.070 -8.383  24.589  1.00 51.67  ? 771  ASN   B CG  1 
ATOM   2821 O  OD1 . ASN   B 1 78  ? 19.318 -9.243  25.424  1.00 52.94  ? 771  ASN   B OD1 1 
ATOM   2822 N  ND2 . ASN   B 1 78  ? 17.865 -7.876  24.472  1.00 53.20  ? 771  ASN   B ND2 1 
ATOM   2823 N  N   . PRO   B 1 79  ? 21.004 -11.299 23.106  1.00 43.93  ? 772  PRO   B N   1 
ATOM   2824 C  CA  . PRO   B 1 79  ? 21.598 -11.680 24.404  1.00 42.89  ? 772  PRO   B CA  1 
ATOM   2825 C  C   . PRO   B 1 79  ? 23.136 -11.680 24.477  1.00 42.19  ? 772  PRO   B C   1 
ATOM   2826 O  O   . PRO   B 1 79  ? 23.711 -11.823 25.553  1.00 42.25  ? 772  PRO   B O   1 
ATOM   2827 C  CB  . PRO   B 1 79  ? 21.005 -13.069 24.639  1.00 43.30  ? 772  PRO   B CB  1 
ATOM   2828 C  CG  . PRO   B 1 79  ? 20.900 -13.646 23.271  1.00 43.96  ? 772  PRO   B CG  1 
ATOM   2829 C  CD  . PRO   B 1 79  ? 20.551 -12.489 22.358  1.00 43.10  ? 772  PRO   B CD  1 
ATOM   2830 N  N   . GLY   B 1 80  ? 23.785 -11.545 23.336  1.00 41.39  ? 773  GLY   B N   1 
ATOM   2831 C  CA  . GLY   B 1 80  ? 25.234 -11.471 23.270  1.00 40.96  ? 773  GLY   B CA  1 
ATOM   2832 C  C   . GLY   B 1 80  ? 25.981 -12.754 22.970  1.00 39.74  ? 773  GLY   B C   1 
ATOM   2833 O  O   . GLY   B 1 80  ? 25.433 -13.852 23.053  1.00 39.60  ? 773  GLY   B O   1 
ATOM   2834 N  N   . ASN   B 1 81  ? 27.259 -12.602 22.623  1.00 38.54  ? 774  ASN   B N   1 
ATOM   2835 C  CA  . ASN   B 1 81  ? 28.132 -13.736 22.393  1.00 37.62  ? 774  ASN   B CA  1 
ATOM   2836 C  C   . ASN   B 1 81  ? 29.548 -13.304 22.764  1.00 36.02  ? 774  ASN   B C   1 
ATOM   2837 O  O   . ASN   B 1 81  ? 30.012 -12.275 22.272  1.00 35.82  ? 774  ASN   B O   1 
ATOM   2838 C  CB  . ASN   B 1 81  ? 28.091 -14.156 20.937  1.00 38.59  ? 774  ASN   B CB  1 
ATOM   2839 C  CG  . ASN   B 1 81  ? 28.735 -15.478 20.708  1.00 40.70  ? 774  ASN   B CG  1 
ATOM   2840 O  OD1 . ASN   B 1 81  ? 28.135 -16.534 20.921  1.00 42.76  ? 774  ASN   B OD1 1 
ATOM   2841 N  ND2 . ASN   B 1 81  ? 29.974 -15.455 20.292  1.00 40.23  ? 774  ASN   B ND2 1 
ATOM   2842 N  N   . PRO   B 1 82  ? 30.269 -14.077 23.598  1.00 34.35  ? 775  PRO   B N   1 
ATOM   2843 C  CA  . PRO   B 1 82  ? 31.625 -13.655 23.975  1.00 33.44  ? 775  PRO   B CA  1 
ATOM   2844 C  C   . PRO   B 1 82  ? 32.605 -13.518 22.818  1.00 32.97  ? 775  PRO   B C   1 
ATOM   2845 O  O   . PRO   B 1 82  ? 33.657 -12.929 23.006  1.00 32.83  ? 775  PRO   B O   1 
ATOM   2846 C  CB  . PRO   B 1 82  ? 32.077 -14.716 24.992  1.00 33.53  ? 775  PRO   B CB  1 
ATOM   2847 C  CG  . PRO   B 1 82  ? 31.150 -15.831 24.854  1.00 33.78  ? 775  PRO   B CG  1 
ATOM   2848 C  CD  . PRO   B 1 82  ? 29.871 -15.325 24.282  1.00 33.01  ? 775  PRO   B CD  1 
ATOM   2849 N  N   . HIS   B 1 83  ? 32.272 -14.042 21.636  1.00 32.61  ? 776  HIS   B N   1 
ATOM   2850 C  CA  . HIS   B 1 83  ? 33.189 -13.986 20.501  1.00 33.08  ? 776  HIS   B CA  1 
ATOM   2851 C  C   . HIS   B 1 83  ? 32.774 -12.979 19.423  1.00 33.85  ? 776  HIS   B C   1 
ATOM   2852 O  O   . HIS   B 1 83  ? 33.206 -13.086 18.284  1.00 32.95  ? 776  HIS   B O   1 
ATOM   2853 C  CB  . HIS   B 1 83  ? 33.419 -15.391 19.924  1.00 32.61  ? 776  HIS   B CB  1 
ATOM   2854 C  CG  . HIS   B 1 83  ? 33.873 -16.347 20.974  1.00 33.68  ? 776  HIS   B CG  1 
ATOM   2855 N  ND1 . HIS   B 1 83  ? 33.079 -17.401 21.375  1.00 35.58  ? 776  HIS   B ND1 1 
ATOM   2856 C  CD2 . HIS   B 1 83  ? 34.974 -16.310 21.757  1.00 34.37  ? 776  HIS   B CD2 1 
ATOM   2857 C  CE1 . HIS   B 1 83  ? 33.743 -18.001 22.346  1.00 35.59  ? 776  HIS   B CE1 1 
ATOM   2858 N  NE2 . HIS   B 1 83  ? 34.887 -17.379 22.612  1.00 35.39  ? 776  HIS   B NE2 1 
ATOM   2859 N  N   . VAL   B 1 84  ? 31.984 -11.972 19.798  1.00 35.09  ? 777  VAL   B N   1 
ATOM   2860 C  CA  . VAL   B 1 84  ? 31.574 -10.890 18.908  1.00 36.71  ? 777  VAL   B CA  1 
ATOM   2861 C  C   . VAL   B 1 84  ? 31.825 -9.577  19.682  1.00 38.42  ? 777  VAL   B C   1 
ATOM   2862 O  O   . VAL   B 1 84  ? 31.417 -9.468  20.842  1.00 38.44  ? 777  VAL   B O   1 
ATOM   2863 C  CB  . VAL   B 1 84  ? 30.095 -11.031 18.463  1.00 37.47  ? 777  VAL   B CB  1 
ATOM   2864 C  CG1 . VAL   B 1 84  ? 29.681 -9.865  17.589  1.00 38.08  ? 777  VAL   B CG1 1 
ATOM   2865 C  CG2 . VAL   B 1 84  ? 29.861 -12.337 17.717  1.00 38.06  ? 777  VAL   B CG2 1 
ATOM   2866 N  N   . CYS   B 1 85  ? 32.527 -8.606  19.068  1.00 39.71  ? 778  CYS   B N   1 
ATOM   2867 C  CA  . CYS   B 1 85  ? 32.823 -7.314  19.697  1.00 41.46  ? 778  CYS   B CA  1 
ATOM   2868 C  C   . CYS   B 1 85  ? 31.565 -6.518  20.047  1.00 43.25  ? 778  CYS   B C   1 
ATOM   2869 O  O   . CYS   B 1 85  ? 30.522 -6.702  19.439  1.00 43.12  ? 778  CYS   B O   1 
ATOM   2870 C  CB  . CYS   B 1 85  ? 33.762 -6.492  18.819  1.00 42.68  ? 778  CYS   B CB  1 
ATOM   2871 S  SG  . CYS   B 1 85  ? 35.453 -7.131  18.745  1.00 48.29  ? 778  CYS   B SG  1 
ATOM   2872 N  N   . ARG   B 1 86  ? 31.658 -5.641  21.039  1.00 44.92  ? 779  ARG   B N   1 
ATOM   2873 C  CA  . ARG   B 1 86  ? 30.537 -4.790  21.429  1.00 46.61  ? 779  ARG   B CA  1 
ATOM   2874 C  C   . ARG   B 1 86  ? 30.814 -3.365  20.941  1.00 46.45  ? 779  ARG   B C   1 
ATOM   2875 O  O   . ARG   B 1 86  ? 31.911 -2.859  21.169  1.00 46.37  ? 779  ARG   B O   1 
ATOM   2876 C  CB  . ARG   B 1 86  ? 30.442 -4.774  22.956  1.00 50.02  ? 779  ARG   B CB  1 
ATOM   2877 C  CG  . ARG   B 1 86  ? 29.081 -4.429  23.516  1.00 56.89  ? 779  ARG   B CG  1 
ATOM   2878 C  CD  . ARG   B 1 86  ? 28.485 -5.671  24.167  1.00 64.31  ? 779  ARG   B CD  1 
ATOM   2879 N  NE  . ARG   B 1 86  ? 27.841 -5.379  25.453  1.00 70.01  ? 779  ARG   B NE  1 
ATOM   2880 C  CZ  . ARG   B 1 86  ? 27.094 -6.247  26.132  1.00 73.23  ? 779  ARG   B CZ  1 
ATOM   2881 N  NH1 . ARG   B 1 86  ? 26.884 -7.473  25.656  1.00 72.64  ? 779  ARG   B NH1 1 
ATOM   2882 N  NH2 . ARG   B 1 86  ? 26.553 -5.898  27.294  1.00 73.70  ? 779  ARG   B NH2 1 
ATOM   2883 N  N   . LEU   B 1 87  ? 29.841 -2.713  20.280  1.00 46.28  ? 780  LEU   B N   1 
ATOM   2884 C  CA  . LEU   B 1 87  ? 30.003 -1.307  19.892  1.00 46.44  ? 780  LEU   B CA  1 
ATOM   2885 C  C   . LEU   B 1 87  ? 29.569 -0.468  21.087  1.00 47.26  ? 780  LEU   B C   1 
ATOM   2886 O  O   . LEU   B 1 87  ? 28.374 -0.411  21.378  1.00 47.61  ? 780  LEU   B O   1 
ATOM   2887 C  CB  . LEU   B 1 87  ? 29.141 -0.949  18.670  1.00 46.21  ? 780  LEU   B CB  1 
ATOM   2888 C  CG  . LEU   B 1 87  ? 29.227 0.515   18.195  1.00 46.47  ? 780  LEU   B CG  1 
ATOM   2889 C  CD1 . LEU   B 1 87  ? 30.635 0.885   17.793  1.00 46.17  ? 780  LEU   B CD1 1 
ATOM   2890 C  CD2 . LEU   B 1 87  ? 28.283 0.775   17.050  1.00 46.98  ? 780  LEU   B CD2 1 
ATOM   2891 N  N   . LEU   B 1 88  ? 30.530 0.140   21.808  1.00 47.48  ? 781  LEU   B N   1 
ATOM   2892 C  CA  . LEU   B 1 88  ? 30.242 0.960   22.986  1.00 48.18  ? 781  LEU   B CA  1 
ATOM   2893 C  C   . LEU   B 1 88  ? 29.507 2.259   22.666  1.00 48.86  ? 781  LEU   B C   1 
ATOM   2894 O  O   . LEU   B 1 88  ? 28.635 2.680   23.423  1.00 49.11  ? 781  LEU   B O   1 
ATOM   2895 C  CB  . LEU   B 1 88  ? 31.532 1.304   23.736  1.00 48.52  ? 781  LEU   B CB  1 
ATOM   2896 C  CG  . LEU   B 1 88  ? 32.247 0.153   24.383  1.00 50.19  ? 781  LEU   B CG  1 
ATOM   2897 C  CD1 . LEU   B 1 88  ? 33.545 0.620   24.986  1.00 51.11  ? 781  LEU   B CD1 1 
ATOM   2898 C  CD2 . LEU   B 1 88  ? 31.393 -0.484  25.451  1.00 50.55  ? 781  LEU   B CD2 1 
ATOM   2899 N  N   . GLY   B 1 89  ? 29.899 2.910   21.582  1.00 49.10  ? 782  GLY   B N   1 
ATOM   2900 C  CA  . GLY   B 1 89  ? 29.297 4.175   21.203  1.00 49.63  ? 782  GLY   B CA  1 
ATOM   2901 C  C   . GLY   B 1 89  ? 29.761 4.701   19.870  1.00 50.01  ? 782  GLY   B C   1 
ATOM   2902 O  O   . GLY   B 1 89  ? 30.725 4.201   19.289  1.00 50.17  ? 782  GLY   B O   1 
ATOM   2903 N  N   . ILE   B 1 90  ? 29.054 5.709   19.373  1.00 50.05  ? 783  ILE   B N   1 
ATOM   2904 C  CA  . ILE   B 1 90  ? 29.364 6.338   18.102  1.00 50.40  ? 783  ILE   B CA  1 
ATOM   2905 C  C   . ILE   B 1 90  ? 29.441 7.848   18.272  1.00 50.55  ? 783  ILE   B C   1 
ATOM   2906 O  O   . ILE   B 1 90  ? 28.700 8.428   19.062  1.00 50.65  ? 783  ILE   B O   1 
ATOM   2907 C  CB  . ILE   B 1 90  ? 28.301 5.935   17.053  1.00 50.88  ? 783  ILE   B CB  1 
ATOM   2908 C  CG1 . ILE   B 1 90  ? 28.648 6.472   15.639  1.00 51.22  ? 783  ILE   B CG1 1 
ATOM   2909 C  CG2 . ILE   B 1 90  ? 26.885 6.339   17.512  1.00 51.38  ? 783  ILE   B CG2 1 
ATOM   2910 C  CD1 . ILE   B 1 90  ? 27.676 6.022   14.531  1.00 52.06  ? 783  ILE   B CD1 1 
ATOM   2911 N  N   . CYS   B 1 91  ? 30.346 8.488   17.542  1.00 50.58  ? 784  CYS   B N   1 
ATOM   2912 C  CA  . CYS   B 1 91  ? 30.470 9.942   17.562  1.00 50.78  ? 784  CYS   B CA  1 
ATOM   2913 C  C   . CYS   B 1 91  ? 30.393 10.463  16.139  1.00 50.92  ? 784  CYS   B C   1 
ATOM   2914 O  O   . CYS   B 1 91  ? 31.309 10.226  15.347  1.00 50.88  ? 784  CYS   B O   1 
ATOM   2915 C  CB  . CYS   B 1 91  ? 31.752 10.392  18.260  1.00 51.06  ? 784  CYS   B CB  1 
ATOM   2916 S  SG  . CYS   B 1 91  ? 31.970 12.193  18.314  1.00 51.64  ? 784  CYS   B SG  1 
ATOM   2917 N  N   . LEU   B 1 92  ? 29.297 11.159  15.809  1.00 51.01  ? 785  LEU   B N   1 
ATOM   2918 C  CA  . LEU   B 1 92  ? 29.115 11.720  14.479  1.00 51.33  ? 785  LEU   B CA  1 
ATOM   2919 C  C   . LEU   B 1 92  ? 29.435 13.205  14.415  1.00 51.01  ? 785  LEU   B C   1 
ATOM   2920 O  O   . LEU   B 1 92  ? 28.795 14.019  15.088  1.00 51.18  ? 785  LEU   B O   1 
ATOM   2921 C  CB  . LEU   B 1 92  ? 27.676 11.513  13.968  1.00 51.76  ? 785  LEU   B CB  1 
ATOM   2922 C  CG  . LEU   B 1 92  ? 27.177 10.082  13.792  1.00 53.35  ? 785  LEU   B CG  1 
ATOM   2923 C  CD1 . LEU   B 1 92  ? 25.812 10.071  13.160  1.00 53.81  ? 785  LEU   B CD1 1 
ATOM   2924 C  CD2 . LEU   B 1 92  ? 28.074 9.284   12.890  1.00 54.10  ? 785  LEU   B CD2 1 
ATOM   2925 N  N   . THR   B 1 93  ? 30.380 13.563  13.546  1.00 50.20  ? 786  THR   B N   1 
ATOM   2926 C  CA  . THR   B 1 93  ? 30.704 14.936  13.188  1.00 49.73  ? 786  THR   B CA  1 
ATOM   2927 C  C   . THR   B 1 93  ? 30.717 14.860  11.624  1.00 49.81  ? 786  THR   B C   1 
ATOM   2928 O  O   . THR   B 1 93  ? 29.769 14.309  11.043  1.00 49.68  ? 786  THR   B O   1 
ATOM   2929 C  CB  . THR   B 1 93  ? 31.978 15.459  13.932  1.00 50.68  ? 786  THR   B CB  1 
ATOM   2930 O  OG1 . THR   B 1 93  ? 33.156 14.885  13.360  1.00 51.31  ? 786  THR   B OG1 1 
ATOM   2931 C  CG2 . THR   B 1 93  ? 31.931 15.281  15.427  1.00 51.13  ? 786  THR   B CG2 1 
ATOM   2932 N  N   . SER   B 1 94  ? 31.770 15.349  10.941  1.00 49.66  ? 787  SER   B N   1 
ATOM   2933 C  CA  . SER   B 1 94  ? 31.899 15.182  9.505   1.00 49.76  ? 787  SER   B CA  1 
ATOM   2934 C  C   . SER   B 1 94  ? 32.331 13.726  9.196   1.00 49.80  ? 787  SER   B C   1 
ATOM   2935 O  O   . SER   B 1 94  ? 32.103 13.249  8.082   1.00 50.73  ? 787  SER   B O   1 
ATOM   2936 C  CB  . SER   B 1 94  ? 32.920 16.170  8.952   1.00 50.78  ? 787  SER   B CB  1 
ATOM   2937 O  OG  . SER   B 1 94  ? 32.552 17.505  9.283   1.00 52.71  ? 787  SER   B OG  1 
ATOM   2938 N  N   . THR   B 1 95  ? 32.959 13.030  10.177  1.00 48.76  ? 788  THR   B N   1 
ATOM   2939 C  CA  . THR   B 1 95  ? 33.386 11.640  10.114  1.00 48.29  ? 788  THR   B CA  1 
ATOM   2940 C  C   . THR   B 1 95  ? 32.596 10.787  11.121  1.00 47.33  ? 788  THR   B C   1 
ATOM   2941 O  O   . THR   B 1 95  ? 32.045 11.299  12.105  1.00 47.12  ? 788  THR   B O   1 
ATOM   2942 C  CB  . THR   B 1 95  ? 34.897 11.534  10.401  1.00 49.63  ? 788  THR   B CB  1 
ATOM   2943 O  OG1 . THR   B 1 95  ? 35.167 11.991  11.734  1.00 49.81  ? 788  THR   B OG1 1 
ATOM   2944 C  CG2 . THR   B 1 95  ? 35.736 12.335  9.388   1.00 50.23  ? 788  THR   B CG2 1 
ATOM   2945 N  N   . VAL   B 1 96  ? 32.553 9.475   10.865  1.00 46.43  ? 789  VAL   B N   1 
ATOM   2946 C  CA  . VAL   B 1 96  ? 31.903 8.520   11.746  1.00 45.78  ? 789  VAL   B CA  1 
ATOM   2947 C  C   . VAL   B 1 96  ? 32.992 7.960   12.641  1.00 45.56  ? 789  VAL   B C   1 
ATOM   2948 O  O   . VAL   B 1 96  ? 34.030 7.509   12.141  1.00 45.73  ? 789  VAL   B O   1 
ATOM   2949 C  CB  . VAL   B 1 96  ? 31.221 7.397   10.943  1.00 46.05  ? 789  VAL   B CB  1 
ATOM   2950 C  CG1 . VAL   B 1 96  ? 30.759 6.261   11.848  1.00 46.37  ? 789  VAL   B CG1 1 
ATOM   2951 C  CG2 . VAL   B 1 96  ? 30.071 7.939   10.113  1.00 46.29  ? 789  VAL   B CG2 1 
ATOM   2952 N  N   . GLN   B 1 97  ? 32.791 8.026   13.963  1.00 44.97  ? 790  GLN   B N   1 
ATOM   2953 C  CA  . GLN   B 1 97  ? 33.766 7.487   14.902  1.00 44.71  ? 790  GLN   B CA  1 
ATOM   2954 C  C   . GLN   B 1 97  ? 33.137 6.359   15.699  1.00 44.73  ? 790  GLN   B C   1 
ATOM   2955 O  O   . GLN   B 1 97  ? 32.141 6.575   16.376  1.00 45.03  ? 790  GLN   B O   1 
ATOM   2956 C  CB  . GLN   B 1 97  ? 34.322 8.584   15.805  1.00 45.34  ? 790  GLN   B CB  1 
ATOM   2957 C  CG  . GLN   B 1 97  ? 35.142 9.593   15.012  1.00 47.05  ? 790  GLN   B CG  1 
ATOM   2958 C  CD  . GLN   B 1 97  ? 36.041 10.418  15.883  1.00 49.14  ? 790  GLN   B CD  1 
ATOM   2959 O  OE1 . GLN   B 1 97  ? 37.155 10.000  16.255  1.00 48.73  ? 790  GLN   B OE1 1 
ATOM   2960 N  NE2 . GLN   B 1 97  ? 35.579 11.611  16.222  1.00 49.62  ? 790  GLN   B NE2 1 
ATOM   2961 N  N   . LEU   B 1 98  ? 33.675 5.139   15.567  1.00 44.08  ? 791  LEU   B N   1 
ATOM   2962 C  CA  . LEU   B 1 98  ? 33.148 3.959   16.244  1.00 43.65  ? 791  LEU   B CA  1 
ATOM   2963 C  C   . LEU   B 1 98  ? 34.029 3.639   17.433  1.00 44.51  ? 791  LEU   B C   1 
ATOM   2964 O  O   . LEU   B 1 98  ? 35.240 3.581   17.289  1.00 44.20  ? 791  LEU   B O   1 
ATOM   2965 C  CB  . LEU   B 1 98  ? 33.100 2.773   15.268  1.00 42.89  ? 791  LEU   B CB  1 
ATOM   2966 C  CG  . LEU   B 1 98  ? 32.266 3.012   14.017  1.00 42.95  ? 791  LEU   B CG  1 
ATOM   2967 C  CD1 . LEU   B 1 98  ? 32.458 1.926   13.012  1.00 43.32  ? 791  LEU   B CD1 1 
ATOM   2968 C  CD2 . LEU   B 1 98  ? 30.817 3.168   14.375  1.00 43.28  ? 791  LEU   B CD2 1 
ATOM   2969 N  N   . ILE   B 1 99  ? 33.431 3.459   18.617  1.00 45.41  ? 792  ILE   B N   1 
ATOM   2970 C  CA  . ILE   B 1 99  ? 34.179 3.221   19.855  1.00 46.12  ? 792  ILE   B CA  1 
ATOM   2971 C  C   . ILE   B 1 99  ? 33.940 1.821   20.408  1.00 47.27  ? 792  ILE   B C   1 
ATOM   2972 O  O   . ILE   B 1 99  ? 32.810 1.349   20.428  1.00 47.46  ? 792  ILE   B O   1 
ATOM   2973 C  CB  . ILE   B 1 99  ? 33.843 4.340   20.882  1.00 46.29  ? 792  ILE   B CB  1 
ATOM   2974 C  CG1 . ILE   B 1 99  ? 34.335 5.716   20.389  1.00 46.72  ? 792  ILE   B CG1 1 
ATOM   2975 C  CG2 . ILE   B 1 99  ? 34.409 4.029   22.266  1.00 46.94  ? 792  ILE   B CG2 1 
ATOM   2976 C  CD1 . ILE   B 1 99  ? 33.298 6.580   19.699  1.00 47.50  ? 792  ILE   B CD1 1 
ATOM   2977 N  N   . THR   B 1 100 ? 35.002 1.137   20.813  1.00 48.13  ? 793  THR   B N   1 
ATOM   2978 C  CA  . THR   B 1 100 ? 34.895 -0.212  21.363  1.00 49.90  ? 793  THR   B CA  1 
ATOM   2979 C  C   . THR   B 1 100 ? 35.952 -0.458  22.453  1.00 51.75  ? 793  THR   B C   1 
ATOM   2980 O  O   . THR   B 1 100 ? 36.867 0.348   22.598  1.00 51.92  ? 793  THR   B O   1 
ATOM   2981 C  CB  . THR   B 1 100 ? 34.961 -1.255  20.231  1.00 51.22  ? 793  THR   B CB  1 
ATOM   2982 O  OG1 . THR   B 1 100 ? 34.296 -2.446  20.661  1.00 52.93  ? 793  THR   B OG1 1 
ATOM   2983 C  CG2 . THR   B 1 100 ? 36.384 -1.581  19.816  1.00 51.20  ? 793  THR   B CG2 1 
ATOM   2984 N  N   . GLN   B 1 101 ? 35.834 -1.561  23.221  1.00 53.00  ? 794  GLN   B N   1 
ATOM   2985 C  CA  . GLN   B 1 101 ? 36.825 -1.877  24.247  1.00 54.93  ? 794  GLN   B CA  1 
ATOM   2986 C  C   . GLN   B 1 101 ? 38.168 -2.181  23.573  1.00 55.99  ? 794  GLN   B C   1 
ATOM   2987 O  O   . GLN   B 1 101 ? 38.199 -2.784  22.498  1.00 56.19  ? 794  GLN   B O   1 
ATOM   2988 C  CB  . GLN   B 1 101 ? 36.361 -3.070  25.094  1.00 57.74  ? 794  GLN   B CB  1 
ATOM   2989 C  CG  . GLN   B 1 101 ? 37.073 -3.201  26.440  1.00 63.64  ? 794  GLN   B CG  1 
ATOM   2990 C  CD  . GLN   B 1 101 ? 37.198 -4.658  26.885  1.00 70.21  ? 794  GLN   B CD  1 
ATOM   2991 O  OE1 . GLN   B 1 101 ? 36.289 -5.488  26.695  1.00 72.15  ? 794  GLN   B OE1 1 
ATOM   2992 N  NE2 . GLN   B 1 101 ? 38.336 -4.996  27.489  1.00 71.15  ? 794  GLN   B NE2 1 
ATOM   2993 N  N   . LEU   B 1 102 ? 39.267 -1.727  24.169  1.00 56.54  ? 795  LEU   B N   1 
ATOM   2994 C  CA  . LEU   B 1 102 ? 40.590 -1.958  23.596  1.00 57.47  ? 795  LEU   B CA  1 
ATOM   2995 C  C   . LEU   B 1 102 ? 41.013 -3.429  23.750  1.00 57.88  ? 795  LEU   B C   1 
ATOM   2996 O  O   . LEU   B 1 102 ? 40.914 -3.980  24.845  1.00 58.45  ? 795  LEU   B O   1 
ATOM   2997 C  CB  . LEU   B 1 102 ? 41.615 -1.018  24.255  1.00 58.19  ? 795  LEU   B CB  1 
ATOM   2998 C  CG  . LEU   B 1 102 ? 43.005 -0.972  23.618  1.00 60.13  ? 795  LEU   B CG  1 
ATOM   2999 C  CD1 . LEU   B 1 102 ? 42.940 -0.502  22.178  1.00 60.60  ? 795  LEU   B CD1 1 
ATOM   3000 C  CD2 . LEU   B 1 102 ? 43.907 -0.049  24.386  1.00 60.96  ? 795  LEU   B CD2 1 
ATOM   3001 N  N   . MET   B 1 103 ? 41.427 -4.079  22.651  1.00 57.48  ? 796  MET   B N   1 
ATOM   3002 C  CA  . MET   B 1 103 ? 41.914 -5.469  22.649  1.00 57.63  ? 796  MET   B CA  1 
ATOM   3003 C  C   . MET   B 1 103 ? 43.418 -5.321  22.644  1.00 58.04  ? 796  MET   B C   1 
ATOM   3004 O  O   . MET   B 1 103 ? 43.961 -4.732  21.703  1.00 58.62  ? 796  MET   B O   1 
ATOM   3005 C  CB  . MET   B 1 103 ? 41.465 -6.190  21.380  1.00 57.87  ? 796  MET   B CB  1 
ATOM   3006 C  CG  . MET   B 1 103 ? 39.977 -6.150  21.176  1.00 59.17  ? 796  MET   B CG  1 
ATOM   3007 S  SD  . MET   B 1 103 ? 39.156 -7.296  22.277  1.00 59.67  ? 796  MET   B SD  1 
ATOM   3008 C  CE  . MET   B 1 103 ? 38.379 -6.180  23.405  1.00 57.26  ? 796  MET   B CE  1 
ATOM   3009 N  N   . PRO   B 1 104 ? 44.107 -5.721  23.729  1.00 57.40  ? 797  PRO   B N   1 
ATOM   3010 C  CA  . PRO   B 1 104 ? 45.545 -5.415  23.824  1.00 56.66  ? 797  PRO   B CA  1 
ATOM   3011 C  C   . PRO   B 1 104 ? 46.445 -6.129  22.830  1.00 55.40  ? 797  PRO   B C   1 
ATOM   3012 O  O   . PRO   B 1 104 ? 47.530 -5.633  22.515  1.00 55.73  ? 797  PRO   B O   1 
ATOM   3013 C  CB  . PRO   B 1 104 ? 45.893 -5.768  25.271  1.00 57.70  ? 797  PRO   B CB  1 
ATOM   3014 C  CG  . PRO   B 1 104 ? 44.588 -5.987  25.983  1.00 58.08  ? 797  PRO   B CG  1 
ATOM   3015 C  CD  . PRO   B 1 104 ? 43.611 -6.395  24.945  1.00 56.68  ? 797  PRO   B CD  1 
ATOM   3016 N  N   . PHE   B 1 105 ? 45.999 -7.277  22.322  1.00 53.89  ? 798  PHE   B N   1 
ATOM   3017 C  CA  . PHE   B 1 105 ? 46.795 -8.048  21.373  1.00 52.62  ? 798  PHE   B CA  1 
ATOM   3018 C  C   . PHE   B 1 105 ? 46.565 -7.691  19.901  1.00 52.54  ? 798  PHE   B C   1 
ATOM   3019 O  O   . PHE   B 1 105 ? 47.210 -8.280  19.037  1.00 53.15  ? 798  PHE   B O   1 
ATOM   3020 C  CB  . PHE   B 1 105 ? 46.584 -9.537  21.612  1.00 51.46  ? 798  PHE   B CB  1 
ATOM   3021 C  CG  . PHE   B 1 105 ? 47.048 -9.973  22.979  1.00 50.92  ? 798  PHE   B CG  1 
ATOM   3022 C  CD1 . PHE   B 1 105 ? 48.358 -10.345 23.196  1.00 51.15  ? 798  PHE   B CD1 1 
ATOM   3023 C  CD2 . PHE   B 1 105 ? 46.176 -9.994  24.048  1.00 51.35  ? 798  PHE   B CD2 1 
ATOM   3024 C  CE1 . PHE   B 1 105 ? 48.781 -10.749 24.449  1.00 51.72  ? 798  PHE   B CE1 1 
ATOM   3025 C  CE2 . PHE   B 1 105 ? 46.604 -10.390 25.304  1.00 51.85  ? 798  PHE   B CE2 1 
ATOM   3026 C  CZ  . PHE   B 1 105 ? 47.903 -10.766 25.497  1.00 51.54  ? 798  PHE   B CZ  1 
ATOM   3027 N  N   . GLY   B 1 106 ? 45.687 -6.725  19.631  1.00 51.76  ? 799  GLY   B N   1 
ATOM   3028 C  CA  . GLY   B 1 106 ? 45.384 -6.297  18.274  1.00 51.77  ? 799  GLY   B CA  1 
ATOM   3029 C  C   . GLY   B 1 106 ? 44.584 -7.351  17.546  1.00 51.62  ? 799  GLY   B C   1 
ATOM   3030 O  O   . GLY   B 1 106 ? 43.757 -8.018  18.172  1.00 52.14  ? 799  GLY   B O   1 
ATOM   3031 N  N   . CYS   B 1 107 ? 44.833 -7.544  16.232  1.00 50.54  ? 800  CYS   B N   1 
ATOM   3032 C  CA  . CYS   B 1 107 ? 44.089 -8.562  15.488  1.00 49.57  ? 800  CYS   B CA  1 
ATOM   3033 C  C   . CYS   B 1 107 ? 44.847 -9.891  15.374  1.00 48.72  ? 800  CYS   B C   1 
ATOM   3034 O  O   . CYS   B 1 107 ? 46.066 -9.938  15.540  1.00 49.12  ? 800  CYS   B O   1 
ATOM   3035 C  CB  . CYS   B 1 107 ? 43.622 -8.048  14.129  1.00 49.63  ? 800  CYS   B CB  1 
ATOM   3036 S  SG  . CYS   B 1 107 ? 44.960 -7.623  12.995  1.00 51.46  ? 800  CYS   B SG  1 
ATOM   3037 N  N   . LEU   B 1 108 ? 44.101 -10.974 15.123  1.00 47.30  ? 801  LEU   B N   1 
ATOM   3038 C  CA  . LEU   B 1 108 ? 44.611 -12.324 14.990  1.00 46.39  ? 801  LEU   B CA  1 
ATOM   3039 C  C   . LEU   B 1 108 ? 45.531 -12.471 13.790  1.00 45.83  ? 801  LEU   B C   1 
ATOM   3040 O  O   . LEU   B 1 108 ? 46.451 -13.274 13.865  1.00 45.91  ? 801  LEU   B O   1 
ATOM   3041 C  CB  . LEU   B 1 108 ? 43.448 -13.322 14.950  1.00 46.30  ? 801  LEU   B CB  1 
ATOM   3042 C  CG  . LEU   B 1 108 ? 43.756 -14.805 15.217  1.00 47.60  ? 801  LEU   B CG  1 
ATOM   3043 C  CD1 . LEU   B 1 108 ? 44.534 -15.009 16.504  1.00 48.10  ? 801  LEU   B CD1 1 
ATOM   3044 C  CD2 . LEU   B 1 108 ? 42.486 -15.617 15.248  1.00 47.94  ? 801  LEU   B CD2 1 
ATOM   3045 N  N   . LEU   B 1 109 ? 45.372 -11.647 12.732  1.00 45.14  ? 802  LEU   B N   1 
ATOM   3046 C  CA  . LEU   B 1 109 ? 46.279 -11.699 11.582  1.00 45.32  ? 802  LEU   B CA  1 
ATOM   3047 C  C   . LEU   B 1 109 ? 47.727 -11.388 12.038  1.00 46.15  ? 802  LEU   B C   1 
ATOM   3048 O  O   . LEU   B 1 109 ? 48.632 -12.193 11.810  1.00 46.26  ? 802  LEU   B O   1 
ATOM   3049 C  CB  . LEU   B 1 109 ? 45.844 -10.700 10.481  1.00 44.78  ? 802  LEU   B CB  1 
ATOM   3050 C  CG  . LEU   B 1 109 ? 46.006 -11.080 8.997   1.00 45.87  ? 802  LEU   B CG  1 
ATOM   3051 C  CD1 . LEU   B 1 109 ? 46.261 -9.864  8.141   1.00 45.87  ? 802  LEU   B CD1 1 
ATOM   3052 C  CD2 . LEU   B 1 109 ? 47.080 -12.155 8.737   1.00 46.59  ? 802  LEU   B CD2 1 
ATOM   3053 N  N   . ASP   B 1 110 ? 47.920 -10.252 12.727  1.00 46.38  ? 803  ASP   B N   1 
ATOM   3054 C  CA  . ASP   B 1 110 ? 49.219 -9.848  13.239  1.00 47.22  ? 803  ASP   B CA  1 
ATOM   3055 C  C   . ASP   B 1 110 ? 49.671 -10.782 14.352  1.00 48.19  ? 803  ASP   B C   1 
ATOM   3056 O  O   . ASP   B 1 110 ? 50.851 -11.111 14.415  1.00 48.73  ? 803  ASP   B O   1 
ATOM   3057 C  CB  . ASP   B 1 110 ? 49.166 -8.410  13.760  1.00 48.57  ? 803  ASP   B CB  1 
ATOM   3058 C  CG  . ASP   B 1 110 ? 48.736 -7.404  12.718  1.00 52.73  ? 803  ASP   B CG  1 
ATOM   3059 O  OD1 . ASP   B 1 110 ? 48.987 -7.650  11.514  1.00 52.88  ? 803  ASP   B OD1 1 
ATOM   3060 O  OD2 . ASP   B 1 110 ? 48.149 -6.369  13.102  1.00 55.23  ? 803  ASP   B OD2 1 
ATOM   3061 N  N   . TYR   B 1 111 ? 48.740 -11.233 15.213  1.00 48.15  ? 804  TYR   B N   1 
ATOM   3062 C  CA  . TYR   B 1 111 ? 49.079 -12.143 16.304  1.00 48.48  ? 804  TYR   B CA  1 
ATOM   3063 C  C   . TYR   B 1 111 ? 49.693 -13.441 15.794  1.00 49.01  ? 804  TYR   B C   1 
ATOM   3064 O  O   . TYR   B 1 111 ? 50.769 -13.806 16.255  1.00 49.21  ? 804  TYR   B O   1 
ATOM   3065 C  CB  . TYR   B 1 111 ? 47.877 -12.415 17.228  1.00 48.44  ? 804  TYR   B CB  1 
ATOM   3066 C  CG  . TYR   B 1 111 ? 48.251 -13.222 18.457  1.00 48.93  ? 804  TYR   B CG  1 
ATOM   3067 C  CD1 . TYR   B 1 111 ? 48.276 -14.609 18.424  1.00 49.51  ? 804  TYR   B CD1 1 
ATOM   3068 C  CD2 . TYR   B 1 111 ? 48.601 -12.596 19.645  1.00 49.83  ? 804  TYR   B CD2 1 
ATOM   3069 C  CE1 . TYR   B 1 111 ? 48.687 -15.349 19.525  1.00 50.62  ? 804  TYR   B CE1 1 
ATOM   3070 C  CE2 . TYR   B 1 111 ? 48.989 -13.327 20.763  1.00 50.49  ? 804  TYR   B CE2 1 
ATOM   3071 C  CZ  . TYR   B 1 111 ? 49.042 -14.705 20.697  1.00 51.38  ? 804  TYR   B CZ  1 
ATOM   3072 O  OH  . TYR   B 1 111 ? 49.429 -15.441 21.795  1.00 52.35  ? 804  TYR   B OH  1 
ATOM   3073 N  N   . VAL   B 1 112 ? 49.042 -14.129 14.839  1.00 49.34  ? 805  VAL   B N   1 
ATOM   3074 C  CA  . VAL   B 1 112 ? 49.587 -15.383 14.307  1.00 50.23  ? 805  VAL   B CA  1 
ATOM   3075 C  C   . VAL   B 1 112 ? 50.895 -15.164 13.530  1.00 51.48  ? 805  VAL   B C   1 
ATOM   3076 O  O   . VAL   B 1 112 ? 51.712 -16.078 13.458  1.00 51.86  ? 805  VAL   B O   1 
ATOM   3077 C  CB  . VAL   B 1 112 ? 48.569 -16.236 13.500  1.00 50.77  ? 805  VAL   B CB  1 
ATOM   3078 C  CG1 . VAL   B 1 112 ? 47.321 -16.528 14.319  1.00 51.22  ? 805  VAL   B CG1 1 
ATOM   3079 C  CG2 . VAL   B 1 112 ? 48.210 -15.592 12.168  1.00 51.07  ? 805  VAL   B CG2 1 
ATOM   3080 N  N   . ARG   B 1 113 ? 51.113 -13.960 12.976  1.00 52.04  ? 806  ARG   B N   1 
ATOM   3081 C  CA  . ARG   B 1 113 ? 52.349 -13.661 12.263  1.00 52.76  ? 806  ARG   B CA  1 
ATOM   3082 C  C   . ARG   B 1 113 ? 53.496 -13.457 13.258  1.00 54.44  ? 806  ARG   B C   1 
ATOM   3083 O  O   . ARG   B 1 113 ? 54.590 -13.978 13.046  1.00 54.81  ? 806  ARG   B O   1 
ATOM   3084 C  CB  . ARG   B 1 113 ? 52.186 -12.410 11.401  1.00 52.42  ? 806  ARG   B CB  1 
ATOM   3085 C  CG  . ARG   B 1 113 ? 51.538 -12.656 10.066  1.00 53.26  ? 806  ARG   B CG  1 
ATOM   3086 C  CD  . ARG   B 1 113 ? 51.295 -11.328 9.393   1.00 54.52  ? 806  ARG   B CD  1 
ATOM   3087 N  NE  . ARG   B 1 113 ? 50.639 -11.470 8.097   1.00 55.53  ? 806  ARG   B NE  1 
ATOM   3088 C  CZ  . ARG   B 1 113 ? 50.105 -10.463 7.412   1.00 56.01  ? 806  ARG   B CZ  1 
ATOM   3089 N  NH1 . ARG   B 1 113 ? 50.139 -9.230  7.897   1.00 54.67  ? 806  ARG   B NH1 1 
ATOM   3090 N  NH2 . ARG   B 1 113 ? 49.530 -10.683 6.240   1.00 55.82  ? 806  ARG   B NH2 1 
ATOM   3091 N  N   . GLU   B 1 114 ? 53.248 -12.710 14.342  1.00 55.29  ? 807  GLU   B N   1 
ATOM   3092 C  CA  . GLU   B 1 114 ? 54.276 -12.421 15.329  1.00 57.05  ? 807  GLU   B CA  1 
ATOM   3093 C  C   . GLU   B 1 114 ? 54.569 -13.580 16.271  1.00 58.84  ? 807  GLU   B C   1 
ATOM   3094 O  O   . GLU   B 1 114 ? 55.688 -13.687 16.773  1.00 59.30  ? 807  GLU   B O   1 
ATOM   3095 C  CB  . GLU   B 1 114 ? 53.930 -11.150 16.103  1.00 59.62  ? 807  GLU   B CB  1 
ATOM   3096 C  CG  . GLU   B 1 114 ? 53.886 -9.940  15.193  1.00 66.02  ? 807  GLU   B CG  1 
ATOM   3097 C  CD  . GLU   B 1 114 ? 53.320 -8.690  15.833  1.00 75.33  ? 807  GLU   B CD  1 
ATOM   3098 O  OE1 . GLU   B 1 114 ? 53.363 -8.594  17.082  1.00 77.93  ? 807  GLU   B OE1 1 
ATOM   3099 O  OE2 . GLU   B 1 114 ? 52.837 -7.805  15.089  1.00 77.32  ? 807  GLU   B OE2 1 
ATOM   3100 N  N   . HIS   B 1 115 ? 53.585 -14.458 16.499  1.00 59.60  ? 808  HIS   B N   1 
ATOM   3101 C  CA  . HIS   B 1 115 ? 53.764 -15.600 17.386  1.00 60.71  ? 808  HIS   B CA  1 
ATOM   3102 C  C   . HIS   B 1 115 ? 53.795 -16.945 16.667  1.00 62.13  ? 808  HIS   B C   1 
ATOM   3103 O  O   . HIS   B 1 115 ? 53.572 -17.969 17.309  1.00 62.26  ? 808  HIS   B O   1 
ATOM   3104 C  CB  . HIS   B 1 115 ? 52.681 -15.604 18.460  1.00 61.16  ? 808  HIS   B CB  1 
ATOM   3105 C  CG  . HIS   B 1 115 ? 52.647 -14.337 19.254  1.00 62.82  ? 808  HIS   B CG  1 
ATOM   3106 N  ND1 . HIS   B 1 115 ? 51.971 -13.221 18.801  1.00 64.55  ? 808  HIS   B ND1 1 
ATOM   3107 C  CD2 . HIS   B 1 115 ? 53.227 -14.042 20.441  1.00 63.88  ? 808  HIS   B CD2 1 
ATOM   3108 C  CE1 . HIS   B 1 115 ? 52.143 -12.293 19.731  1.00 64.88  ? 808  HIS   B CE1 1 
ATOM   3109 N  NE2 . HIS   B 1 115 ? 52.885 -12.743 20.739  1.00 64.76  ? 808  HIS   B NE2 1 
ATOM   3110 N  N   . LYS   B 1 116 ? 54.107 -16.939 15.351  1.00 62.94  ? 809  LYS   B N   1 
ATOM   3111 C  CA  . LYS   B 1 116 ? 54.200 -18.080 14.423  1.00 64.06  ? 809  LYS   B CA  1 
ATOM   3112 C  C   . LYS   B 1 116 ? 54.900 -19.323 14.999  1.00 65.27  ? 809  LYS   B C   1 
ATOM   3113 O  O   . LYS   B 1 116 ? 54.456 -20.452 14.777  1.00 65.61  ? 809  LYS   B O   1 
ATOM   3114 C  CB  . LYS   B 1 116 ? 54.923 -17.616 13.145  1.00 65.87  ? 809  LYS   B CB  1 
ATOM   3115 C  CG  . LYS   B 1 116 ? 55.042 -18.676 12.070  1.00 70.27  ? 809  LYS   B CG  1 
ATOM   3116 C  CD  . LYS   B 1 116 ? 56.486 -19.083 11.795  1.00 75.30  ? 809  LYS   B CD  1 
ATOM   3117 C  CE  . LYS   B 1 116 ? 56.571 -20.312 10.918  1.00 79.17  ? 809  LYS   B CE  1 
ATOM   3118 N  NZ  . LYS   B 1 116 ? 56.009 -21.514 11.591  1.00 81.43  ? 809  LYS   B NZ  1 
ATOM   3119 N  N   . ASP   B 1 117 ? 56.002 -19.109 15.732  1.00 65.88  ? 810  ASP   B N   1 
ATOM   3120 C  CA  . ASP   B 1 117 ? 56.807 -20.178 16.306  1.00 66.94  ? 810  ASP   B CA  1 
ATOM   3121 C  C   . ASP   B 1 117 ? 56.406 -20.573 17.736  1.00 67.28  ? 810  ASP   B C   1 
ATOM   3122 O  O   . ASP   B 1 117 ? 57.130 -21.347 18.366  1.00 67.92  ? 810  ASP   B O   1 
ATOM   3123 C  CB  . ASP   B 1 117 ? 58.302 -19.834 16.223  1.00 69.36  ? 810  ASP   B CB  1 
ATOM   3124 C  CG  . ASP   B 1 117 ? 58.806 -19.722 14.798  1.00 75.71  ? 810  ASP   B CG  1 
ATOM   3125 O  OD1 . ASP   B 1 117 ? 58.733 -20.739 14.058  1.00 77.75  ? 810  ASP   B OD1 1 
ATOM   3126 O  OD2 . ASP   B 1 117 ? 59.269 -18.617 14.415  1.00 77.44  ? 810  ASP   B OD2 1 
ATOM   3127 N  N   . ASN   B 1 118 ? 55.269 -20.078 18.248  1.00 66.46  ? 811  ASN   B N   1 
ATOM   3128 C  CA  . ASN   B 1 118 ? 54.791 -20.508 19.563  1.00 66.16  ? 811  ASN   B CA  1 
ATOM   3129 C  C   . ASN   B 1 118 ? 53.277 -20.801 19.590  1.00 64.66  ? 811  ASN   B C   1 
ATOM   3130 O  O   . ASN   B 1 118 ? 52.675 -20.823 20.671  1.00 64.90  ? 811  ASN   B O   1 
ATOM   3131 C  CB  . ASN   B 1 118 ? 55.201 -19.570 20.696  1.00 68.34  ? 811  ASN   B CB  1 
ATOM   3132 C  CG  . ASN   B 1 118 ? 55.391 -20.321 22.004  1.00 72.59  ? 811  ASN   B CG  1 
ATOM   3133 O  OD1 . ASN   B 1 118 ? 56.346 -21.101 22.177  1.00 73.51  ? 811  ASN   B OD1 1 
ATOM   3134 N  ND2 . ASN   B 1 118 ? 54.460 -20.130 22.938  1.00 73.80  ? 811  ASN   B ND2 1 
ATOM   3135 N  N   . ILE   B 1 119 ? 52.673 -21.067 18.407  1.00 62.70  ? 812  ILE   B N   1 
ATOM   3136 C  CA  . ILE   B 1 119 ? 51.263 -21.423 18.299  1.00 61.03  ? 812  ILE   B CA  1 
ATOM   3137 C  C   . ILE   B 1 119 ? 51.137 -22.926 18.012  1.00 59.48  ? 812  ILE   B C   1 
ATOM   3138 O  O   . ILE   B 1 119 ? 51.758 -23.448 17.087  1.00 59.32  ? 812  ILE   B O   1 
ATOM   3139 C  CB  . ILE   B 1 119 ? 50.530 -20.540 17.261  1.00 61.19  ? 812  ILE   B CB  1 
ATOM   3140 C  CG1 . ILE   B 1 119 ? 50.559 -19.064 17.681  1.00 61.66  ? 812  ILE   B CG1 1 
ATOM   3141 C  CG2 . ILE   B 1 119 ? 49.108 -21.002 17.072  1.00 61.73  ? 812  ILE   B CG2 1 
ATOM   3142 C  CD1 . ILE   B 1 119 ? 50.170 -18.137 16.622  1.00 62.69  ? 812  ILE   B CD1 1 
ATOM   3143 N  N   . GLY   B 1 120 ? 50.382 -23.614 18.854  1.00 58.31  ? 813  GLY   B N   1 
ATOM   3144 C  CA  . GLY   B 1 120 ? 50.173 -25.044 18.712  1.00 57.43  ? 813  GLY   B CA  1 
ATOM   3145 C  C   . GLY   B 1 120 ? 48.840 -25.386 18.086  1.00 56.29  ? 813  GLY   B C   1 
ATOM   3146 O  O   . GLY   B 1 120 ? 48.059 -24.501 17.721  1.00 56.21  ? 813  GLY   B O   1 
ATOM   3147 N  N   . SER   B 1 121 ? 48.573 -26.684 17.954  1.00 55.30  ? 814  SER   B N   1 
ATOM   3148 C  CA  . SER   B 1 121 ? 47.342 -27.170 17.345  1.00 54.80  ? 814  SER   B CA  1 
ATOM   3149 C  C   . SER   B 1 121 ? 46.115 -26.890 18.191  1.00 54.15  ? 814  SER   B C   1 
ATOM   3150 O  O   . SER   B 1 121 ? 45.039 -26.710 17.634  1.00 54.14  ? 814  SER   B O   1 
ATOM   3151 C  CB  . SER   B 1 121 ? 47.442 -28.659 17.027  1.00 55.96  ? 814  SER   B CB  1 
ATOM   3152 O  OG  . SER   B 1 121 ? 48.017 -29.392 18.095  1.00 58.26  ? 814  SER   B OG  1 
ATOM   3153 N  N   . GLN   B 1 122 ? 46.268 -26.858 19.529  1.00 53.33  ? 815  GLN   B N   1 
ATOM   3154 C  CA  . GLN   B 1 122 ? 45.167 -26.604 20.457  1.00 52.58  ? 815  GLN   B CA  1 
ATOM   3155 C  C   . GLN   B 1 122 ? 44.646 -25.181 20.288  1.00 50.27  ? 815  GLN   B C   1 
ATOM   3156 O  O   . GLN   B 1 122 ? 43.440 -24.973 20.287  1.00 50.01  ? 815  GLN   B O   1 
ATOM   3157 C  CB  . GLN   B 1 122 ? 45.617 -26.862 21.913  1.00 55.39  ? 815  GLN   B CB  1 
ATOM   3158 C  CG  . GLN   B 1 122 ? 44.529 -26.694 22.974  1.00 61.41  ? 815  GLN   B CG  1 
ATOM   3159 C  CD  . GLN   B 1 122 ? 43.541 -27.841 23.015  1.00 70.31  ? 815  GLN   B CD  1 
ATOM   3160 O  OE1 . GLN   B 1 122 ? 43.699 -28.813 23.771  1.00 72.86  ? 815  GLN   B OE1 1 
ATOM   3161 N  NE2 . GLN   B 1 122 ? 42.482 -27.747 22.215  1.00 71.99  ? 815  GLN   B NE2 1 
ATOM   3162 N  N   . TYR   B 1 123 ? 45.548 -24.212 20.100  1.00 48.59  ? 816  TYR   B N   1 
ATOM   3163 C  CA  . TYR   B 1 123 ? 45.162 -22.814 19.923  1.00 47.43  ? 816  TYR   B CA  1 
ATOM   3164 C  C   . TYR   B 1 123 ? 44.497 -22.551 18.588  1.00 45.25  ? 816  TYR   B C   1 
ATOM   3165 O  O   . TYR   B 1 123 ? 43.417 -21.973 18.561  1.00 44.94  ? 816  TYR   B O   1 
ATOM   3166 C  CB  . TYR   B 1 123 ? 46.351 -21.868 20.160  1.00 47.94  ? 816  TYR   B CB  1 
ATOM   3167 C  CG  . TYR   B 1 123 ? 46.501 -21.510 21.623  1.00 49.64  ? 816  TYR   B CG  1 
ATOM   3168 C  CD1 . TYR   B 1 123 ? 46.924 -22.450 22.548  1.00 50.92  ? 816  TYR   B CD1 1 
ATOM   3169 C  CD2 . TYR   B 1 123 ? 46.134 -20.256 22.098  1.00 50.93  ? 816  TYR   B CD2 1 
ATOM   3170 C  CE1 . TYR   B 1 123 ? 47.009 -22.145 23.903  1.00 51.78  ? 816  TYR   B CE1 1 
ATOM   3171 C  CE2 . TYR   B 1 123 ? 46.228 -19.937 23.448  1.00 51.84  ? 816  TYR   B CE2 1 
ATOM   3172 C  CZ  . TYR   B 1 123 ? 46.656 -20.890 24.349  1.00 52.61  ? 816  TYR   B CZ  1 
ATOM   3173 O  OH  . TYR   B 1 123 ? 46.762 -20.598 25.684  1.00 54.39  ? 816  TYR   B OH  1 
ATOM   3174 N  N   . LEU   B 1 124 ? 45.111 -22.999 17.482  1.00 43.81  ? 817  LEU   B N   1 
ATOM   3175 C  CA  . LEU   B 1 124 ? 44.549 -22.803 16.146  1.00 42.93  ? 817  LEU   B CA  1 
ATOM   3176 C  C   . LEU   B 1 124 ? 43.134 -23.382 16.022  1.00 41.82  ? 817  LEU   B C   1 
ATOM   3177 O  O   . LEU   B 1 124 ? 42.218 -22.682 15.601  1.00 41.80  ? 817  LEU   B O   1 
ATOM   3178 C  CB  . LEU   B 1 124 ? 45.460 -23.425 15.087  1.00 43.23  ? 817  LEU   B CB  1 
ATOM   3179 C  CG  . LEU   B 1 124 ? 46.788 -22.765 14.874  1.00 44.43  ? 817  LEU   B CG  1 
ATOM   3180 C  CD1 . LEU   B 1 124 ? 47.716 -23.701 14.155  1.00 45.10  ? 817  LEU   B CD1 1 
ATOM   3181 C  CD2 . LEU   B 1 124 ? 46.635 -21.483 14.094  1.00 44.71  ? 817  LEU   B CD2 1 
ATOM   3182 N  N   . LEU   B 1 125 ? 42.947 -24.636 16.436  1.00 40.96  ? 818  LEU   B N   1 
ATOM   3183 C  CA  . LEU   B 1 125 ? 41.657 -25.300 16.379  1.00 40.46  ? 818  LEU   B CA  1 
ATOM   3184 C  C   . LEU   B 1 125 ? 40.632 -24.627 17.284  1.00 40.08  ? 818  LEU   B C   1 
ATOM   3185 O  O   . LEU   B 1 125 ? 39.478 -24.487 16.892  1.00 40.20  ? 818  LEU   B O   1 
ATOM   3186 C  CB  . LEU   B 1 125 ? 41.825 -26.788 16.714  1.00 40.53  ? 818  LEU   B CB  1 
ATOM   3187 C  CG  . LEU   B 1 125 ? 42.566 -27.600 15.642  1.00 41.40  ? 818  LEU   B CG  1 
ATOM   3188 C  CD1 . LEU   B 1 125 ? 42.887 -28.997 16.127  1.00 41.72  ? 818  LEU   B CD1 1 
ATOM   3189 C  CD2 . LEU   B 1 125 ? 41.772 -27.635 14.348  1.00 41.67  ? 818  LEU   B CD2 1 
ATOM   3190 N  N   . ASN   B 1 126 ? 41.059 -24.145 18.455  1.00 39.68  ? 819  ASN   B N   1 
ATOM   3191 C  CA  . ASN   B 1 126 ? 40.156 -23.447 19.368  1.00 39.64  ? 819  ASN   B CA  1 
ATOM   3192 C  C   . ASN   B 1 126 ? 39.750 -22.082 18.850  1.00 39.80  ? 819  ASN   B C   1 
ATOM   3193 O  O   . ASN   B 1 126 ? 38.649 -21.634 19.148  1.00 39.58  ? 819  ASN   B O   1 
ATOM   3194 C  CB  . ASN   B 1 126 ? 40.734 -23.348 20.761  1.00 40.43  ? 819  ASN   B CB  1 
ATOM   3195 C  CG  . ASN   B 1 126 ? 40.398 -24.520 21.637  1.00 42.41  ? 819  ASN   B CG  1 
ATOM   3196 O  OD1 . ASN   B 1 126 ? 39.249 -24.974 21.696  1.00 43.70  ? 819  ASN   B OD1 1 
ATOM   3197 N  ND2 . ASN   B 1 126 ? 41.394 -25.021 22.347  1.00 42.32  ? 819  ASN   B ND2 1 
ATOM   3198 N  N   . TRP   B 1 127 ? 40.614 -21.421 18.058  1.00 40.15  ? 820  TRP   B N   1 
ATOM   3199 C  CA  . TRP   B 1 127 ? 40.250 -20.142 17.455  1.00 40.49  ? 820  TRP   B CA  1 
ATOM   3200 C  C   . TRP   B 1 127 ? 39.196 -20.389 16.370  1.00 39.85  ? 820  TRP   B C   1 
ATOM   3201 O  O   . TRP   B 1 127 ? 38.253 -19.614 16.263  1.00 40.48  ? 820  TRP   B O   1 
ATOM   3202 C  CB  . TRP   B 1 127 ? 41.471 -19.410 16.899  1.00 41.25  ? 820  TRP   B CB  1 
ATOM   3203 C  CG  . TRP   B 1 127 ? 42.413 -18.901 17.950  1.00 43.22  ? 820  TRP   B CG  1 
ATOM   3204 C  CD1 . TRP   B 1 127 ? 42.091 -18.458 19.204  1.00 44.90  ? 820  TRP   B CD1 1 
ATOM   3205 C  CD2 . TRP   B 1 127 ? 43.829 -18.715 17.811  1.00 43.89  ? 820  TRP   B CD2 1 
ATOM   3206 N  NE1 . TRP   B 1 127 ? 43.225 -18.047 19.869  1.00 45.42  ? 820  TRP   B NE1 1 
ATOM   3207 C  CE2 . TRP   B 1 127 ? 44.308 -18.200 19.037  1.00 45.05  ? 820  TRP   B CE2 1 
ATOM   3208 C  CE3 . TRP   B 1 127 ? 44.744 -18.956 16.776  1.00 44.23  ? 820  TRP   B CE3 1 
ATOM   3209 C  CZ2 . TRP   B 1 127 ? 45.658 -17.934 19.256  1.00 45.48  ? 820  TRP   B CZ2 1 
ATOM   3210 C  CZ3 . TRP   B 1 127 ? 46.079 -18.699 17.002  1.00 45.00  ? 820  TRP   B CZ3 1 
ATOM   3211 C  CH2 . TRP   B 1 127 ? 46.524 -18.190 18.225  1.00 45.32  ? 820  TRP   B CH2 1 
ATOM   3212 N  N   . CYS   B 1 128 ? 39.307 -21.501 15.618  1.00 38.28  ? 821  CYS   B N   1 
ATOM   3213 C  CA  . CYS   B 1 128 ? 38.329 -21.867 14.607  1.00 37.58  ? 821  CYS   B CA  1 
ATOM   3214 C  C   . CYS   B 1 128 ? 36.944 -22.084 15.219  1.00 37.10  ? 821  CYS   B C   1 
ATOM   3215 O  O   . CYS   B 1 128 ? 35.940 -21.736 14.599  1.00 37.14  ? 821  CYS   B O   1 
ATOM   3216 C  CB  . CYS   B 1 128 ? 38.801 -23.093 13.841  1.00 38.08  ? 821  CYS   B CB  1 
ATOM   3217 S  SG  . CYS   B 1 128 ? 40.290 -22.802 12.866  1.00 41.26  ? 821  CYS   B SG  1 
ATOM   3218 N  N   . VAL   B 1 129 ? 36.884 -22.642 16.434  1.00 36.28  ? 822  VAL   B N   1 
ATOM   3219 C  CA  . VAL   B 1 129 ? 35.624 -22.835 17.138  1.00 35.81  ? 822  VAL   B CA  1 
ATOM   3220 C  C   . VAL   B 1 129 ? 35.043 -21.486 17.551  1.00 35.81  ? 822  VAL   B C   1 
ATOM   3221 O  O   . VAL   B 1 129 ? 33.878 -21.239 17.282  1.00 36.28  ? 822  VAL   B O   1 
ATOM   3222 C  CB  . VAL   B 1 129 ? 35.786 -23.741 18.363  1.00 36.30  ? 822  VAL   B CB  1 
ATOM   3223 C  CG1 . VAL   B 1 129 ? 34.466 -23.885 19.103  1.00 36.75  ? 822  VAL   B CG1 1 
ATOM   3224 C  CG2 . VAL   B 1 129 ? 36.330 -25.101 17.966  1.00 36.92  ? 822  VAL   B CG2 1 
ATOM   3225 N  N   . GLN   B 1 130 ? 35.849 -20.601 18.172  1.00 35.28  ? 823  GLN   B N   1 
ATOM   3226 C  CA  . GLN   B 1 130 ? 35.388 -19.285 18.620  1.00 35.24  ? 823  GLN   B CA  1 
ATOM   3227 C  C   . GLN   B 1 130 ? 34.870 -18.414 17.487  1.00 34.76  ? 823  GLN   B C   1 
ATOM   3228 O  O   . GLN   B 1 130 ? 33.789 -17.855 17.613  1.00 34.74  ? 823  GLN   B O   1 
ATOM   3229 C  CB  . GLN   B 1 130 ? 36.478 -18.575 19.425  1.00 37.05  ? 823  GLN   B CB  1 
ATOM   3230 C  CG  . GLN   B 1 130 ? 36.897 -19.382 20.641  1.00 40.55  ? 823  GLN   B CG  1 
ATOM   3231 C  CD  . GLN   B 1 130 ? 37.872 -18.667 21.543  1.00 46.38  ? 823  GLN   B CD  1 
ATOM   3232 O  OE1 . GLN   B 1 130 ? 38.205 -17.495 21.363  1.00 48.41  ? 823  GLN   B OE1 1 
ATOM   3233 N  NE2 . GLN   B 1 130 ? 38.349 -19.368 22.552  1.00 47.68  ? 823  GLN   B NE2 1 
ATOM   3234 N  N   . ILE   B 1 131 ? 35.587 -18.351 16.359  1.00 34.55  ? 824  ILE   B N   1 
ATOM   3235 C  CA  . ILE   B 1 131 ? 35.136 -17.584 15.199  1.00 34.61  ? 824  ILE   B CA  1 
ATOM   3236 C  C   . ILE   B 1 131 ? 33.814 -18.136 14.646  1.00 34.69  ? 824  ILE   B C   1 
ATOM   3237 O  O   . ILE   B 1 131 ? 32.925 -17.365 14.302  1.00 34.85  ? 824  ILE   B O   1 
ATOM   3238 C  CB  . ILE   B 1 131 ? 36.233 -17.527 14.121  1.00 34.99  ? 824  ILE   B CB  1 
ATOM   3239 C  CG1 . ILE   B 1 131 ? 37.523 -16.904 14.694  1.00 36.16  ? 824  ILE   B CG1 1 
ATOM   3240 C  CG2 . ILE   B 1 131 ? 35.736 -16.778 12.896  1.00 35.22  ? 824  ILE   B CG2 1 
ATOM   3241 C  CD1 . ILE   B 1 131 ? 38.737 -17.118 13.875  1.00 37.53  ? 824  ILE   B CD1 1 
ATOM   3242 N  N   . ALA   B 1 132 ? 33.667 -19.467 14.607  1.00 34.54  ? 825  ALA   B N   1 
ATOM   3243 C  CA  . ALA   B 1 132 ? 32.436 -20.101 14.129  1.00 34.72  ? 825  ALA   B CA  1 
ATOM   3244 C  C   . ALA   B 1 132 ? 31.277 -19.884 15.126  1.00 34.80  ? 825  ALA   B C   1 
ATOM   3245 O  O   . ALA   B 1 132 ? 30.126 -19.785 14.715  1.00 34.52  ? 825  ALA   B O   1 
ATOM   3246 C  CB  . ALA   B 1 132 ? 32.669 -21.584 13.878  1.00 34.71  ? 825  ALA   B CB  1 
ATOM   3247 N  N   . LYS   B 1 133 ? 31.590 -19.801 16.433  1.00 34.78  ? 826  LYS   B N   1 
ATOM   3248 C  CA  . LYS   B 1 133 ? 30.626 -19.534 17.503  1.00 34.73  ? 826  LYS   B CA  1 
ATOM   3249 C  C   . LYS   B 1 133 ? 30.108 -18.095 17.372  1.00 35.60  ? 826  LYS   B C   1 
ATOM   3250 O  O   . LYS   B 1 133 ? 28.911 -17.859 17.514  1.00 36.20  ? 826  LYS   B O   1 
ATOM   3251 C  CB  . LYS   B 1 133 ? 31.267 -19.746 18.883  1.00 34.42  ? 826  LYS   B CB  1 
ATOM   3252 C  CG  . LYS   B 1 133 ? 31.374 -21.199 19.305  1.00 34.95  ? 826  LYS   B CG  1 
ATOM   3253 C  CD  . LYS   B 1 133 ? 32.108 -21.309 20.616  1.00 36.33  ? 826  LYS   B CD  1 
ATOM   3254 C  CE  . LYS   B 1 133 ? 31.812 -22.604 21.308  1.00 38.66  ? 826  LYS   B CE  1 
ATOM   3255 N  NZ  . LYS   B 1 133 ? 32.744 -22.819 22.438  1.00 39.90  ? 826  LYS   B NZ  1 
ATOM   3256 N  N   . GLY   B 1 134 ? 31.005 -17.160 17.071  1.00 35.23  ? 827  GLY   B N   1 
ATOM   3257 C  CA  . GLY   B 1 134 ? 30.644 -15.770 16.879  1.00 35.81  ? 827  GLY   B CA  1 
ATOM   3258 C  C   . GLY   B 1 134 ? 29.816 -15.552 15.629  1.00 36.89  ? 827  GLY   B C   1 
ATOM   3259 O  O   . GLY   B 1 134 ? 28.805 -14.846 15.673  1.00 37.74  ? 827  GLY   B O   1 
ATOM   3260 N  N   . MET   B 1 135 ? 30.228 -16.181 14.499  1.00 36.38  ? 828  MET   B N   1 
ATOM   3261 C  CA  . MET   B 1 135 ? 29.544 -16.092 13.211  1.00 35.83  ? 828  MET   B CA  1 
ATOM   3262 C  C   . MET   B 1 135 ? 28.176 -16.775 13.228  1.00 36.61  ? 828  MET   B C   1 
ATOM   3263 O  O   . MET   B 1 135 ? 27.217 -16.282 12.635  1.00 36.93  ? 828  MET   B O   1 
ATOM   3264 C  CB  . MET   B 1 135 ? 30.426 -16.664 12.100  1.00 35.46  ? 828  MET   B CB  1 
ATOM   3265 C  CG  . MET   B 1 135 ? 31.626 -15.815 11.769  1.00 35.73  ? 828  MET   B CG  1 
ATOM   3266 S  SD  . MET   B 1 135 ? 31.187 -14.142 11.226  1.00 36.50  ? 828  MET   B SD  1 
ATOM   3267 C  CE  . MET   B 1 135 ? 30.558 -14.479 9.634   1.00 34.05  ? 828  MET   B CE  1 
ATOM   3268 N  N   . ASN   B 1 136 ? 28.076 -17.896 13.935  1.00 37.00  ? 829  ASN   B N   1 
ATOM   3269 C  CA  . ASN   B 1 136 ? 26.820 -18.619 14.109  1.00 37.90  ? 829  ASN   B CA  1 
ATOM   3270 C  C   . ASN   B 1 136 ? 25.840 -17.719 14.893  1.00 37.89  ? 829  ASN   B C   1 
ATOM   3271 O  O   . ASN   B 1 136 ? 24.661 -17.669 14.553  1.00 38.54  ? 829  ASN   B O   1 
ATOM   3272 C  CB  . ASN   B 1 136 ? 27.088 -19.929 14.861  1.00 39.84  ? 829  ASN   B CB  1 
ATOM   3273 C  CG  . ASN   B 1 136 ? 25.874 -20.663 15.355  1.00 44.60  ? 829  ASN   B CG  1 
ATOM   3274 O  OD1 . ASN   B 1 136 ? 25.039 -21.137 14.576  1.00 46.85  ? 829  ASN   B OD1 1 
ATOM   3275 N  ND2 . ASN   B 1 136 ? 25.770 -20.786 16.672  1.00 45.50  ? 829  ASN   B ND2 1 
ATOM   3276 N  N   . TYR   B 1 137 ? 26.337 -16.974 15.898  1.00 36.78  ? 830  TYR   B N   1 
ATOM   3277 C  CA  . TYR   B 1 137 ? 25.503 -16.061 16.650  1.00 36.40  ? 830  TYR   B CA  1 
ATOM   3278 C  C   . TYR   B 1 137 ? 25.009 -14.935 15.735  1.00 37.33  ? 830  TYR   B C   1 
ATOM   3279 O  O   . TYR   B 1 137 ? 23.837 -14.578 15.820  1.00 38.73  ? 830  TYR   B O   1 
ATOM   3280 C  CB  . TYR   B 1 137 ? 26.250 -15.501 17.865  1.00 35.36  ? 830  TYR   B CB  1 
ATOM   3281 C  CG  . TYR   B 1 137 ? 25.464 -14.421 18.563  1.00 34.88  ? 830  TYR   B CG  1 
ATOM   3282 C  CD1 . TYR   B 1 137 ? 24.350 -14.732 19.328  1.00 35.39  ? 830  TYR   B CD1 1 
ATOM   3283 C  CD2 . TYR   B 1 137 ? 25.801 -13.084 18.415  1.00 35.15  ? 830  TYR   B CD2 1 
ATOM   3284 C  CE1 . TYR   B 1 137 ? 23.604 -13.743 19.959  1.00 36.00  ? 830  TYR   B CE1 1 
ATOM   3285 C  CE2 . TYR   B 1 137 ? 25.064 -12.086 19.037  1.00 36.02  ? 830  TYR   B CE2 1 
ATOM   3286 C  CZ  . TYR   B 1 137 ? 23.974 -12.420 19.828  1.00 37.01  ? 830  TYR   B CZ  1 
ATOM   3287 O  OH  . TYR   B 1 137 ? 23.216 -11.435 20.424  1.00 38.98  ? 830  TYR   B OH  1 
ATOM   3288 N  N   . LEU   B 1 138 ? 25.871 -14.385 14.853  1.00 36.11  ? 831  LEU   B N   1 
ATOM   3289 C  CA  . LEU   B 1 138 ? 25.441 -13.338 13.930  1.00 35.90  ? 831  LEU   B CA  1 
ATOM   3290 C  C   . LEU   B 1 138 ? 24.376 -13.886 12.981  1.00 37.31  ? 831  LEU   B C   1 
ATOM   3291 O  O   . LEU   B 1 138 ? 23.441 -13.163 12.665  1.00 37.34  ? 831  LEU   B O   1 
ATOM   3292 C  CB  . LEU   B 1 138 ? 26.616 -12.785 13.111  1.00 35.42  ? 831  LEU   B CB  1 
ATOM   3293 C  CG  . LEU   B 1 138 ? 27.691 -11.999 13.848  1.00 36.38  ? 831  LEU   B CG  1 
ATOM   3294 C  CD1 . LEU   B 1 138 ? 28.723 -11.442 12.871  1.00 35.99  ? 831  LEU   B CD1 1 
ATOM   3295 C  CD2 . LEU   B 1 138 ? 27.084 -10.857 14.670  1.00 37.23  ? 831  LEU   B CD2 1 
ATOM   3296 N  N   . GLU   B 1 139 ? 24.500 -15.177 12.554  1.00 38.13  ? 832  GLU   B N   1 
ATOM   3297 C  CA  . GLU   B 1 139 ? 23.529 -15.853 11.691  1.00 39.05  ? 832  GLU   B CA  1 
ATOM   3298 C  C   . GLU   B 1 139 ? 22.180 -15.937 12.416  1.00 41.37  ? 832  GLU   B C   1 
ATOM   3299 O  O   . GLU   B 1 139 ? 21.141 -15.624 11.822  1.00 42.39  ? 832  GLU   B O   1 
ATOM   3300 C  CB  . GLU   B 1 139 ? 24.024 -17.249 11.289  1.00 39.36  ? 832  GLU   B CB  1 
ATOM   3301 C  CG  . GLU   B 1 139 ? 22.995 -18.042 10.497  1.00 41.67  ? 832  GLU   B CG  1 
ATOM   3302 C  CD  . GLU   B 1 139 ? 23.498 -19.200 9.659   1.00 46.56  ? 832  GLU   B CD  1 
ATOM   3303 O  OE1 . GLU   B 1 139 ? 24.612 -19.702 9.928   1.00 45.71  ? 832  GLU   B OE1 1 
ATOM   3304 O  OE2 . GLU   B 1 139 ? 22.772 -19.604 8.721   1.00 50.57  ? 832  GLU   B OE2 1 
ATOM   3305 N  N   . ASP   B 1 140 ? 22.208 -16.296 13.710  1.00 41.59  ? 833  ASP   B N   1 
ATOM   3306 C  CA  . ASP   B 1 140 ? 21.030 -16.375 14.570  1.00 42.51  ? 833  ASP   B CA  1 
ATOM   3307 C  C   . ASP   B 1 140 ? 20.328 -15.014 14.651  1.00 44.28  ? 833  ASP   B C   1 
ATOM   3308 O  O   . ASP   B 1 140 ? 19.099 -14.930 14.630  1.00 44.52  ? 833  ASP   B O   1 
ATOM   3309 C  CB  . ASP   B 1 140 ? 21.456 -16.835 15.976  1.00 43.19  ? 833  ASP   B CB  1 
ATOM   3310 C  CG  . ASP   B 1 140 ? 20.313 -17.004 16.942  1.00 46.32  ? 833  ASP   B CG  1 
ATOM   3311 O  OD1 . ASP   B 1 140 ? 19.704 -18.096 16.954  1.00 47.05  ? 833  ASP   B OD1 1 
ATOM   3312 O  OD2 . ASP   B 1 140 ? 20.036 -16.056 17.694  1.00 47.44  ? 833  ASP   B OD2 1 
ATOM   3313 N  N   . ARG   B 1 141 ? 21.123 -13.949 14.735  1.00 45.23  ? 834  ARG   B N   1 
ATOM   3314 C  CA  . ARG   B 1 141 ? 20.661 -12.575 14.795  1.00 46.58  ? 834  ARG   B CA  1 
ATOM   3315 C  C   . ARG   B 1 141 ? 20.230 -12.016 13.416  1.00 47.70  ? 834  ARG   B C   1 
ATOM   3316 O  O   . ARG   B 1 141 ? 19.918 -10.831 13.330  1.00 47.88  ? 834  ARG   B O   1 
ATOM   3317 C  CB  . ARG   B 1 141 ? 21.790 -11.711 15.390  1.00 48.01  ? 834  ARG   B CB  1 
ATOM   3318 C  CG  . ARG   B 1 141 ? 21.486 -11.118 16.761  1.00 50.84  ? 834  ARG   B CG  1 
ATOM   3319 C  CD  . ARG   B 1 141 ? 21.092 -12.148 17.790  1.00 53.41  ? 834  ARG   B CD  1 
ATOM   3320 N  NE  . ARG   B 1 141 ? 19.823 -11.801 18.418  1.00 56.60  ? 834  ARG   B NE  1 
ATOM   3321 C  CZ  . ARG   B 1 141 ? 18.980 -12.683 18.945  1.00 58.85  ? 834  ARG   B CZ  1 
ATOM   3322 N  NH1 . ARG   B 1 141 ? 17.844 -12.278 19.492  1.00 60.37  ? 834  ARG   B NH1 1 
ATOM   3323 N  NH2 . ARG   B 1 141 ? 19.268 -13.976 18.930  1.00 56.78  ? 834  ARG   B NH2 1 
ATOM   3324 N  N   . ARG   B 1 142 ? 20.220 -12.856 12.355  1.00 48.33  ? 835  ARG   B N   1 
ATOM   3325 C  CA  . ARG   B 1 142 ? 19.857 -12.505 10.983  1.00 49.25  ? 835  ARG   B CA  1 
ATOM   3326 C  C   . ARG   B 1 142 ? 20.767 -11.386 10.441  1.00 48.87  ? 835  ARG   B C   1 
ATOM   3327 O  O   . ARG   B 1 142 ? 20.292 -10.461 9.778   1.00 49.30  ? 835  ARG   B O   1 
ATOM   3328 C  CB  . ARG   B 1 142 ? 18.355 -12.138 10.870  1.00 52.08  ? 835  ARG   B CB  1 
ATOM   3329 C  CG  . ARG   B 1 142 ? 17.375 -13.257 11.287  1.00 57.14  ? 835  ARG   B CG  1 
ATOM   3330 C  CD  . ARG   B 1 142 ? 16.486 -12.870 12.478  1.00 62.22  ? 835  ARG   B CD  1 
ATOM   3331 N  NE  . ARG   B 1 142 ? 15.704 -11.654 12.226  1.00 67.31  ? 835  ARG   B NE  1 
ATOM   3332 C  CZ  . ARG   B 1 142 ? 15.796 -10.527 12.940  1.00 70.20  ? 835  ARG   B CZ  1 
ATOM   3333 N  NH1 . ARG   B 1 142 ? 15.054 -9.470  12.625  1.00 69.21  ? 835  ARG   B NH1 1 
ATOM   3334 N  NH2 . ARG   B 1 142 ? 16.632 -10.451 13.972  1.00 70.22  ? 835  ARG   B NH2 1 
ATOM   3335 N  N   . LEU   B 1 143 ? 22.077 -11.471 10.731  1.00 47.79  ? 836  LEU   B N   1 
ATOM   3336 C  CA  . LEU   B 1 143 ? 23.043 -10.463 10.297  1.00 46.92  ? 836  LEU   B CA  1 
ATOM   3337 C  C   . LEU   B 1 143 ? 24.139 -11.070 9.412   1.00 45.62  ? 836  LEU   B C   1 
ATOM   3338 O  O   . LEU   B 1 143 ? 24.822 -11.994 9.842   1.00 45.68  ? 836  LEU   B O   1 
ATOM   3339 C  CB  . LEU   B 1 143 ? 23.692 -9.828  11.538  1.00 47.49  ? 836  LEU   B CB  1 
ATOM   3340 C  CG  . LEU   B 1 143 ? 24.219 -8.398  11.404  1.00 49.75  ? 836  LEU   B CG  1 
ATOM   3341 C  CD1 . LEU   B 1 143 ? 24.083 -7.662  12.692  1.00 50.38  ? 836  LEU   B CD1 1 
ATOM   3342 C  CD2 . LEU   B 1 143 ? 25.681 -8.363  10.952  1.00 50.79  ? 836  LEU   B CD2 1 
ATOM   3343 N  N   . VAL   B 1 144 ? 24.338 -10.535 8.202   1.00 44.33  ? 837  VAL   B N   1 
ATOM   3344 C  CA  . VAL   B 1 144 ? 25.419 -10.987 7.330   1.00 43.35  ? 837  VAL   B CA  1 
ATOM   3345 C  C   . VAL   B 1 144 ? 26.595 -10.033 7.563   1.00 43.41  ? 837  VAL   B C   1 
ATOM   3346 O  O   . VAL   B 1 144 ? 26.410 -8.811  7.535   1.00 43.80  ? 837  VAL   B O   1 
ATOM   3347 C  CB  . VAL   B 1 144 ? 24.981 -11.006 5.854   1.00 42.93  ? 837  VAL   B CB  1 
ATOM   3348 C  CG1 . VAL   B 1 144 ? 26.131 -11.401 4.937   1.00 43.17  ? 837  VAL   B CG1 1 
ATOM   3349 C  CG2 . VAL   B 1 144 ? 23.798 -11.934 5.666   1.00 43.13  ? 837  VAL   B CG2 1 
ATOM   3350 N  N   . HIS   B 1 145 ? 27.783 -10.583 7.847   1.00 42.72  ? 838  HIS   B N   1 
ATOM   3351 C  CA  . HIS   B 1 145 ? 28.987 -9.803  8.125   1.00 42.65  ? 838  HIS   B CA  1 
ATOM   3352 C  C   . HIS   B 1 145 ? 29.506 -9.034  6.878   1.00 42.51  ? 838  HIS   B C   1 
ATOM   3353 O  O   . HIS   B 1 145 ? 29.666 -7.808  6.925   1.00 42.50  ? 838  HIS   B O   1 
ATOM   3354 C  CB  . HIS   B 1 145 ? 30.074 -10.722 8.717   1.00 43.16  ? 838  HIS   B CB  1 
ATOM   3355 C  CG  . HIS   B 1 145 ? 31.212 -10.000 9.362   1.00 45.21  ? 838  HIS   B CG  1 
ATOM   3356 N  ND1 . HIS   B 1 145 ? 32.090 -9.229  8.625   1.00 47.04  ? 838  HIS   B ND1 1 
ATOM   3357 C  CD2 . HIS   B 1 145 ? 31.604 -9.988  10.656  1.00 46.53  ? 838  HIS   B CD2 1 
ATOM   3358 C  CE1 . HIS   B 1 145 ? 32.966 -8.747  9.489   1.00 47.63  ? 838  HIS   B CE1 1 
ATOM   3359 N  NE2 . HIS   B 1 145 ? 32.711 -9.171  10.726  1.00 47.71  ? 838  HIS   B NE2 1 
ATOM   3360 N  N   . ARG   B 1 146 ? 29.786 -9.772  5.786   1.00 41.89  ? 839  ARG   B N   1 
ATOM   3361 C  CA  . ARG   B 1 146 ? 30.301 -9.283  4.511   1.00 41.52  ? 839  ARG   B CA  1 
ATOM   3362 C  C   . ARG   B 1 146 ? 31.787 -8.975  4.507   1.00 41.21  ? 839  ARG   B C   1 
ATOM   3363 O  O   . ARG   B 1 146 ? 32.294 -8.596  3.452   1.00 41.81  ? 839  ARG   B O   1 
ATOM   3364 C  CB  . ARG   B 1 146 ? 29.518 -8.086  3.986   1.00 43.01  ? 839  ARG   B CB  1 
ATOM   3365 C  CG  . ARG   B 1 146 ? 28.086 -8.395  3.678   1.00 47.11  ? 839  ARG   B CG  1 
ATOM   3366 C  CD  . ARG   B 1 146 ? 27.280 -7.125  3.612   1.00 52.42  ? 839  ARG   B CD  1 
ATOM   3367 N  NE  . ARG   B 1 146 ? 25.977 -7.293  4.258   1.00 58.26  ? 839  ARG   B NE  1 
ATOM   3368 C  CZ  . ARG   B 1 146 ? 24.815 -7.289  3.610   1.00 62.21  ? 839  ARG   B CZ  1 
ATOM   3369 N  NH1 . ARG   B 1 146 ? 23.675 -7.462  4.277   1.00 62.20  ? 839  ARG   B NH1 1 
ATOM   3370 N  NH2 . ARG   B 1 146 ? 24.780 -7.106  2.289   1.00 61.89  ? 839  ARG   B NH2 1 
ATOM   3371 N  N   . ASP   B 1 147 ? 32.496 -9.139  5.633   1.00 40.40  ? 840  ASP   B N   1 
ATOM   3372 C  CA  . ASP   B 1 147 ? 33.923 -8.844  5.659   1.00 40.63  ? 840  ASP   B CA  1 
ATOM   3373 C  C   . ASP   B 1 147 ? 34.682 -9.630  6.708   1.00 40.25  ? 840  ASP   B C   1 
ATOM   3374 O  O   . ASP   B 1 147 ? 35.504 -9.068  7.437   1.00 40.45  ? 840  ASP   B O   1 
ATOM   3375 C  CB  . ASP   B 1 147 ? 34.177 -7.337  5.795   1.00 43.30  ? 840  ASP   B CB  1 
ATOM   3376 C  CG  . ASP   B 1 147 ? 35.593 -6.935  5.418   1.00 51.21  ? 840  ASP   B CG  1 
ATOM   3377 O  OD1 . ASP   B 1 147 ? 36.251 -7.696  4.666   1.00 52.32  ? 840  ASP   B OD1 1 
ATOM   3378 O  OD2 . ASP   B 1 147 ? 36.055 -5.865  5.888   1.00 55.24  ? 840  ASP   B OD2 1 
ATOM   3379 N  N   . LEU   B 1 148 ? 34.407 -10.933 6.799   1.00 39.61  ? 841  LEU   B N   1 
ATOM   3380 C  CA  . LEU   B 1 148 ? 35.112 -11.769 7.766   1.00 39.22  ? 841  LEU   B CA  1 
ATOM   3381 C  C   . LEU   B 1 148 ? 36.481 -12.087 7.204   1.00 38.54  ? 841  LEU   B C   1 
ATOM   3382 O  O   . LEU   B 1 148 ? 36.594 -12.516 6.064   1.00 39.29  ? 841  LEU   B O   1 
ATOM   3383 C  CB  . LEU   B 1 148 ? 34.339 -13.042 8.101   1.00 39.46  ? 841  LEU   B CB  1 
ATOM   3384 C  CG  . LEU   B 1 148 ? 35.038 -13.994 9.053   1.00 40.99  ? 841  LEU   B CG  1 
ATOM   3385 C  CD1 . LEU   B 1 148 ? 35.318 -13.335 10.415  1.00 41.66  ? 841  LEU   B CD1 1 
ATOM   3386 C  CD2 . LEU   B 1 148 ? 34.245 -15.245 9.215   1.00 41.37  ? 841  LEU   B CD2 1 
ATOM   3387 N  N   . ALA   B 1 149 ? 37.515 -11.801 7.965   1.00 37.15  ? 842  ALA   B N   1 
ATOM   3388 C  CA  . ALA   B 1 149 ? 38.902 -12.034 7.594   1.00 36.76  ? 842  ALA   B CA  1 
ATOM   3389 C  C   . ALA   B 1 149 ? 39.715 -12.133 8.884   1.00 36.46  ? 842  ALA   B C   1 
ATOM   3390 O  O   . ALA   B 1 149 ? 39.216 -11.722 9.926   1.00 36.13  ? 842  ALA   B O   1 
ATOM   3391 C  CB  . ALA   B 1 149 ? 39.404 -10.875 6.742   1.00 36.80  ? 842  ALA   B CB  1 
ATOM   3392 N  N   . ALA   B 1 150 ? 40.958 -12.650 8.842   1.00 36.66  ? 843  ALA   B N   1 
ATOM   3393 C  CA  . ALA   B 1 150 ? 41.783 -12.729 10.054  1.00 37.57  ? 843  ALA   B CA  1 
ATOM   3394 C  C   . ALA   B 1 150 ? 42.082 -11.339 10.633  1.00 38.40  ? 843  ALA   B C   1 
ATOM   3395 O  O   . ALA   B 1 150 ? 42.268 -11.207 11.841  1.00 38.43  ? 843  ALA   B O   1 
ATOM   3396 C  CB  . ALA   B 1 150 ? 43.065 -13.490 9.786   1.00 37.91  ? 843  ALA   B CB  1 
ATOM   3397 N  N   . ARG   B 1 151 ? 42.062 -10.294 9.781   1.00 38.92  ? 844  ARG   B N   1 
ATOM   3398 C  CA  . ARG   B 1 151 ? 42.236 -8.911  10.211  1.00 39.47  ? 844  ARG   B CA  1 
ATOM   3399 C  C   . ARG   B 1 151 ? 41.031 -8.425  11.030  1.00 39.53  ? 844  ARG   B C   1 
ATOM   3400 O  O   . ARG   B 1 151 ? 41.184 -7.520  11.825  1.00 39.65  ? 844  ARG   B O   1 
ATOM   3401 C  CB  . ARG   B 1 151 ? 42.476 -7.984  9.004   1.00 40.81  ? 844  ARG   B CB  1 
ATOM   3402 C  CG  . ARG   B 1 151 ? 41.269 -7.846  8.086   1.00 44.27  ? 844  ARG   B CG  1 
ATOM   3403 C  CD  . ARG   B 1 151 ? 41.467 -6.884  6.910   1.00 47.66  ? 844  ARG   B CD  1 
ATOM   3404 N  NE  . ARG   B 1 151 ? 40.308 -6.907  6.004   1.00 50.45  ? 844  ARG   B NE  1 
ATOM   3405 C  CZ  . ARG   B 1 151 ? 40.176 -7.751  4.985   1.00 52.06  ? 844  ARG   B CZ  1 
ATOM   3406 N  NH1 . ARG   B 1 151 ? 39.084 -7.726  4.233   1.00 51.12  ? 844  ARG   B NH1 1 
ATOM   3407 N  NH2 . ARG   B 1 151 ? 41.137 -8.625  4.707   1.00 51.57  ? 844  ARG   B NH2 1 
ATOM   3408 N  N   . ASN   B 1 152 ? 39.844 -9.012  10.847  1.00 39.58  ? 845  ASN   B N   1 
ATOM   3409 C  CA  . ASN   B 1 152 ? 38.637 -8.608  11.575  1.00 40.44  ? 845  ASN   B CA  1 
ATOM   3410 C  C   . ASN   B 1 152 ? 38.266 -9.541  12.746  1.00 40.63  ? 845  ASN   B C   1 
ATOM   3411 O  O   . ASN   B 1 152 ? 37.114 -9.606  13.172  1.00 40.81  ? 845  ASN   B O   1 
ATOM   3412 C  CB  . ASN   B 1 152 ? 37.463 -8.422  10.613  1.00 41.42  ? 845  ASN   B CB  1 
ATOM   3413 C  CG  . ASN   B 1 152 ? 37.670 -7.263  9.674   1.00 43.64  ? 845  ASN   B CG  1 
ATOM   3414 O  OD1 . ASN   B 1 152 ? 37.361 -7.338  8.491   1.00 45.56  ? 845  ASN   B OD1 1 
ATOM   3415 N  ND2 . ASN   B 1 152 ? 38.218 -6.177  10.160  1.00 42.92  ? 845  ASN   B ND2 1 
ATOM   3416 N  N   . VAL   B 1 153 ? 39.251 -10.248 13.261  1.00 40.27  ? 846  VAL   B N   1 
ATOM   3417 C  CA  . VAL   B 1 153 ? 39.096 -11.098 14.411  1.00 40.91  ? 846  VAL   B CA  1 
ATOM   3418 C  C   . VAL   B 1 153 ? 40.110 -10.512 15.377  1.00 42.01  ? 846  VAL   B C   1 
ATOM   3419 O  O   . VAL   B 1 153 ? 41.295 -10.464 15.060  1.00 42.90  ? 846  VAL   B O   1 
ATOM   3420 C  CB  . VAL   B 1 153 ? 39.399 -12.576 14.092  1.00 41.08  ? 846  VAL   B CB  1 
ATOM   3421 C  CG1 . VAL   B 1 153 ? 39.374 -13.408 15.363  1.00 41.57  ? 846  VAL   B CG1 1 
ATOM   3422 C  CG2 . VAL   B 1 153 ? 38.411 -13.127 13.064  1.00 41.33  ? 846  VAL   B CG2 1 
ATOM   3423 N  N   . LEU   B 1 154 ? 39.648 -9.980  16.507  1.00 41.54  ? 847  LEU   B N   1 
ATOM   3424 C  CA  . LEU   B 1 154 ? 40.527 -9.340  17.464  1.00 41.54  ? 847  LEU   B CA  1 
ATOM   3425 C  C   . LEU   B 1 154 ? 40.867 -10.260 18.618  1.00 42.13  ? 847  LEU   B C   1 
ATOM   3426 O  O   . LEU   B 1 154 ? 40.105 -11.161 18.951  1.00 41.98  ? 847  LEU   B O   1 
ATOM   3427 C  CB  . LEU   B 1 154 ? 39.939 -8.009  17.936  1.00 41.54  ? 847  LEU   B CB  1 
ATOM   3428 C  CG  . LEU   B 1 154 ? 39.376 -7.084  16.823  1.00 42.93  ? 847  LEU   B CG  1 
ATOM   3429 C  CD1 . LEU   B 1 154 ? 38.790 -5.838  17.375  1.00 43.97  ? 847  LEU   B CD1 1 
ATOM   3430 C  CD2 . LEU   B 1 154 ? 40.414 -6.720  15.815  1.00 43.11  ? 847  LEU   B CD2 1 
ATOM   3431 N  N   . VAL   B 1 155 ? 42.031 -10.055 19.221  1.00 42.55  ? 848  VAL   B N   1 
ATOM   3432 C  CA  . VAL   B 1 155 ? 42.508 -10.906 20.319  1.00 42.90  ? 848  VAL   B CA  1 
ATOM   3433 C  C   . VAL   B 1 155 ? 42.392 -10.207 21.676  1.00 43.46  ? 848  VAL   B C   1 
ATOM   3434 O  O   . VAL   B 1 155 ? 43.184 -9.314  21.973  1.00 43.82  ? 848  VAL   B O   1 
ATOM   3435 C  CB  . VAL   B 1 155 ? 43.961 -11.380 20.064  1.00 43.11  ? 848  VAL   B CB  1 
ATOM   3436 C  CG1 . VAL   B 1 155 ? 44.410 -12.384 21.113  1.00 43.49  ? 848  VAL   B CG1 1 
ATOM   3437 C  CG2 . VAL   B 1 155 ? 44.112 -11.960 18.667  1.00 43.39  ? 848  VAL   B CG2 1 
ATOM   3438 N  N   . LYS   B 1 156 ? 41.410 -10.610 22.502  1.00 43.10  ? 849  LYS   B N   1 
ATOM   3439 C  CA  . LYS   B 1 156 ? 41.250 -10.051 23.839  1.00 42.81  ? 849  LYS   B CA  1 
ATOM   3440 C  C   . LYS   B 1 156 ? 42.367 -10.630 24.711  1.00 43.10  ? 849  LYS   B C   1 
ATOM   3441 O  O   . LYS   B 1 156 ? 43.094 -9.891  25.358  1.00 43.74  ? 849  LYS   B O   1 
ATOM   3442 C  CB  . LYS   B 1 156 ? 39.867 -10.390 24.392  1.00 44.01  ? 849  LYS   B CB  1 
ATOM   3443 C  CG  . LYS   B 1 156 ? 39.596 -9.799  25.763  1.00 46.73  ? 849  LYS   B CG  1 
ATOM   3444 C  CD  . LYS   B 1 156 ? 38.108 -9.741  26.013  1.00 50.34  ? 849  LYS   B CD  1 
ATOM   3445 C  CE  . LYS   B 1 156 ? 37.773 -9.012  27.277  1.00 54.14  ? 849  LYS   B CE  1 
ATOM   3446 N  NZ  . LYS   B 1 156 ? 37.675 -9.951  28.420  1.00 56.74  ? 849  LYS   B NZ  1 
ATOM   3447 N  N   . THR   B 1 157 ? 42.516 -11.958 24.688  1.00 42.74  ? 850  THR   B N   1 
ATOM   3448 C  CA  . THR   B 1 157 ? 43.577 -12.758 25.316  1.00 42.72  ? 850  THR   B CA  1 
ATOM   3449 C  C   . THR   B 1 157 ? 43.944 -13.854 24.293  1.00 42.17  ? 850  THR   B C   1 
ATOM   3450 O  O   . THR   B 1 157 ? 43.119 -14.162 23.420  1.00 42.22  ? 850  THR   B O   1 
ATOM   3451 C  CB  . THR   B 1 157 ? 43.138 -13.382 26.677  1.00 43.89  ? 850  THR   B CB  1 
ATOM   3452 O  OG1 . THR   B 1 157 ? 42.310 -14.526 26.488  1.00 44.88  ? 850  THR   B OG1 1 
ATOM   3453 C  CG2 . THR   B 1 157 ? 42.450 -12.402 27.593  1.00 44.40  ? 850  THR   B CG2 1 
ATOM   3454 N  N   . PRO   B 1 158 ? 45.114 -14.521 24.399  1.00 41.34  ? 851  PRO   B N   1 
ATOM   3455 C  CA  . PRO   B 1 158 ? 45.423 -15.606 23.435  1.00 40.83  ? 851  PRO   B CA  1 
ATOM   3456 C  C   . PRO   B 1 158 ? 44.353 -16.702 23.363  1.00 40.51  ? 851  PRO   B C   1 
ATOM   3457 O  O   . PRO   B 1 158 ? 44.244 -17.380 22.343  1.00 41.40  ? 851  PRO   B O   1 
ATOM   3458 C  CB  . PRO   B 1 158 ? 46.768 -16.149 23.922  1.00 41.29  ? 851  PRO   B CB  1 
ATOM   3459 C  CG  . PRO   B 1 158 ? 47.381 -14.982 24.635  1.00 41.81  ? 851  PRO   B CG  1 
ATOM   3460 C  CD  . PRO   B 1 158 ? 46.228 -14.309 25.340  1.00 40.34  ? 851  PRO   B CD  1 
ATOM   3461 N  N   . GLN   B 1 159 ? 43.533 -16.842 24.409  1.00 39.22  ? 852  GLN   B N   1 
ATOM   3462 C  CA  . GLN   B 1 159 ? 42.459 -17.812 24.418  1.00 39.10  ? 852  GLN   B CA  1 
ATOM   3463 C  C   . GLN   B 1 159 ? 41.057 -17.203 24.283  1.00 38.72  ? 852  GLN   B C   1 
ATOM   3464 O  O   . GLN   B 1 159 ? 40.075 -17.890 24.553  1.00 39.34  ? 852  GLN   B O   1 
ATOM   3465 C  CB  . GLN   B 1 159 ? 42.537 -18.737 25.648  1.00 40.95  ? 852  GLN   B CB  1 
ATOM   3466 C  CG  . GLN   B 1 159 ? 42.769 -18.064 26.971  1.00 44.37  ? 852  GLN   B CG  1 
ATOM   3467 C  CD  . GLN   B 1 159 ? 44.235 -17.905 27.295  1.00 47.67  ? 852  GLN   B CD  1 
ATOM   3468 O  OE1 . GLN   B 1 159 ? 44.631 -16.886 27.862  1.00 49.94  ? 852  GLN   B OE1 1 
ATOM   3469 N  NE2 . GLN   B 1 159 ? 45.071 -18.885 26.943  1.00 45.62  ? 852  GLN   B NE2 1 
ATOM   3470 N  N   . HIS   B 1 160 ? 40.947 -15.948 23.853  1.00 37.68  ? 853  HIS   B N   1 
ATOM   3471 C  CA  . HIS   B 1 160 ? 39.650 -15.294 23.694  1.00 37.23  ? 853  HIS   B CA  1 
ATOM   3472 C  C   . HIS   B 1 160 ? 39.672 -14.339 22.495  1.00 36.95  ? 853  HIS   B C   1 
ATOM   3473 O  O   . HIS   B 1 160 ? 40.187 -13.226 22.593  1.00 36.74  ? 853  HIS   B O   1 
ATOM   3474 C  CB  . HIS   B 1 160 ? 39.245 -14.567 24.981  1.00 37.33  ? 853  HIS   B CB  1 
ATOM   3475 C  CG  . HIS   B 1 160 ? 37.858 -14.003 24.982  1.00 39.63  ? 853  HIS   B CG  1 
ATOM   3476 N  ND1 . HIS   B 1 160 ? 37.248 -13.591 26.164  1.00 42.02  ? 853  HIS   B ND1 1 
ATOM   3477 C  CD2 . HIS   B 1 160 ? 37.005 -13.789 23.955  1.00 40.24  ? 853  HIS   B CD2 1 
ATOM   3478 C  CE1 . HIS   B 1 160 ? 36.047 -13.161 25.815  1.00 42.08  ? 853  HIS   B CE1 1 
ATOM   3479 N  NE2 . HIS   B 1 160 ? 35.858 -13.259 24.497  1.00 41.40  ? 853  HIS   B NE2 1 
ATOM   3480 N  N   . VAL   B 1 161 ? 39.097 -14.780 21.371  1.00 36.52  ? 854  VAL   B N   1 
ATOM   3481 C  CA  . VAL   B 1 161 ? 39.018 -13.988 20.153  1.00 36.72  ? 854  VAL   B CA  1 
ATOM   3482 C  C   . VAL   B 1 161 ? 37.580 -13.511 19.916  1.00 36.84  ? 854  VAL   B C   1 
ATOM   3483 O  O   . VAL   B 1 161 ? 36.635 -14.160 20.355  1.00 36.72  ? 854  VAL   B O   1 
ATOM   3484 C  CB  . VAL   B 1 161 ? 39.654 -14.668 18.898  1.00 37.20  ? 854  VAL   B CB  1 
ATOM   3485 C  CG1 . VAL   B 1 161 ? 41.060 -15.192 19.190  1.00 37.38  ? 854  VAL   B CG1 1 
ATOM   3486 C  CG2 . VAL   B 1 161 ? 38.770 -15.777 18.346  1.00 37.81  ? 854  VAL   B CG2 1 
ATOM   3487 N  N   . LYS   B 1 162 ? 37.427 -12.335 19.268  1.00 36.73  ? 855  LYS   B N   1 
ATOM   3488 C  CA  . LYS   B 1 162 ? 36.135 -11.713 18.982  1.00 36.73  ? 855  LYS   B CA  1 
ATOM   3489 C  C   . LYS   B 1 162 ? 36.071 -11.191 17.554  1.00 37.69  ? 855  LYS   B C   1 
ATOM   3490 O  O   . LYS   B 1 162 ? 37.067 -10.729 17.026  1.00 38.13  ? 855  LYS   B O   1 
ATOM   3491 C  CB  . LYS   B 1 162 ? 35.902 -10.536 19.933  1.00 37.26  ? 855  LYS   B CB  1 
ATOM   3492 C  CG  . LYS   B 1 162 ? 35.675 -10.939 21.365  1.00 38.16  ? 855  LYS   B CG  1 
ATOM   3493 C  CD  . LYS   B 1 162 ? 36.073 -9.836  22.281  1.00 39.12  ? 855  LYS   B CD  1 
ATOM   3494 C  CE  . LYS   B 1 162 ? 35.223 -9.836  23.523  1.00 42.43  ? 855  LYS   B CE  1 
ATOM   3495 N  NZ  . LYS   B 1 162 ? 33.826 -9.390  23.261  1.00 44.28  ? 855  LYS   B NZ  1 
ATOM   3496 N  N   . ILE   B 1 163 ? 34.887 -11.213 16.941  1.00 37.77  ? 856  ILE   B N   1 
ATOM   3497 C  CA  . ILE   B 1 163 ? 34.686 -10.714 15.580  1.00 37.56  ? 856  ILE   B CA  1 
ATOM   3498 C  C   . ILE   B 1 163 ? 34.248 -9.246  15.594  1.00 39.03  ? 856  ILE   B C   1 
ATOM   3499 O  O   . ILE   B 1 163 ? 33.248 -8.878  16.230  1.00 39.06  ? 856  ILE   B O   1 
ATOM   3500 C  CB  . ILE   B 1 163 ? 33.658 -11.586 14.845  1.00 36.58  ? 856  ILE   B CB  1 
ATOM   3501 C  CG1 . ILE   B 1 163 ? 34.140 -13.025 14.769  1.00 36.67  ? 856  ILE   B CG1 1 
ATOM   3502 C  CG2 . ILE   B 1 163 ? 33.353 -11.025 13.456  1.00 36.83  ? 856  ILE   B CG2 1 
ATOM   3503 C  CD1 . ILE   B 1 163 ? 33.098 -13.941 14.471  1.00 37.66  ? 856  ILE   B CD1 1 
ATOM   3504 N  N   . THR   B 1 164 ? 34.995 -8.409  14.877  1.00 40.03  ? 857  THR   B N   1 
ATOM   3505 C  CA  . THR   B 1 164 ? 34.683 -6.986  14.763  1.00 40.99  ? 857  THR   B CA  1 
ATOM   3506 C  C   . THR   B 1 164 ? 34.179 -6.644  13.333  1.00 41.67  ? 857  THR   B C   1 
ATOM   3507 O  O   . THR   B 1 164 ? 34.162 -7.501  12.456  1.00 41.32  ? 857  THR   B O   1 
ATOM   3508 C  CB  . THR   B 1 164 ? 35.936 -6.162  15.146  1.00 42.17  ? 857  THR   B CB  1 
ATOM   3509 O  OG1 . THR   B 1 164 ? 35.562 -4.799  15.114  1.00 43.25  ? 857  THR   B OG1 1 
ATOM   3510 C  CG2 . THR   B 1 164 ? 37.056 -6.319  14.150  1.00 42.56  ? 857  THR   B CG2 1 
ATOM   3511 N  N   . ASP   B 1 165 ? 33.760 -5.399  13.119  1.00 42.56  ? 858  ASP   B N   1 
ATOM   3512 C  CA  . ASP   B 1 165 ? 33.368 -4.837  11.841  1.00 43.78  ? 858  ASP   B CA  1 
ATOM   3513 C  C   . ASP   B 1 165 ? 32.111 -5.438  11.244  1.00 44.58  ? 858  ASP   B C   1 
ATOM   3514 O  O   . ASP   B 1 165 ? 31.899 -5.300  10.038  1.00 45.21  ? 858  ASP   B O   1 
ATOM   3515 C  CB  . ASP   B 1 165 ? 34.536 -4.859  10.833  1.00 45.40  ? 858  ASP   B CB  1 
ATOM   3516 C  CG  . ASP   B 1 165 ? 35.619 -3.832  11.134  1.00 49.55  ? 858  ASP   B CG  1 
ATOM   3517 O  OD1 . ASP   B 1 165 ? 35.672 -3.345  12.274  1.00 50.26  ? 858  ASP   B OD1 1 
ATOM   3518 O  OD2 . ASP   B 1 165 ? 36.412 -3.520  10.224  1.00 52.03  ? 858  ASP   B OD2 1 
ATOM   3519 N  N   . PHE   B 1 166 ? 31.247 -6.023  12.070  1.00 44.59  ? 859  PHE   B N   1 
ATOM   3520 C  CA  . PHE   B 1 166 ? 29.955 -6.504  11.586  1.00 45.43  ? 859  PHE   B CA  1 
ATOM   3521 C  C   . PHE   B 1 166 ? 29.080 -5.262  11.405  1.00 46.49  ? 859  PHE   B C   1 
ATOM   3522 O  O   . PHE   B 1 166 ? 29.125 -4.339  12.225  1.00 46.51  ? 859  PHE   B O   1 
ATOM   3523 C  CB  . PHE   B 1 166 ? 29.296 -7.499  12.565  1.00 45.10  ? 859  PHE   B CB  1 
ATOM   3524 C  CG  . PHE   B 1 166 ? 29.280 -7.034  14.000  1.00 45.54  ? 859  PHE   B CG  1 
ATOM   3525 C  CD1 . PHE   B 1 166 ? 30.369 -7.257  14.832  1.00 46.23  ? 859  PHE   B CD1 1 
ATOM   3526 C  CD2 . PHE   B 1 166 ? 28.176 -6.379  14.522  1.00 46.22  ? 859  PHE   B CD2 1 
ATOM   3527 C  CE1 . PHE   B 1 166 ? 30.364 -6.800  16.143  1.00 46.99  ? 859  PHE   B CE1 1 
ATOM   3528 C  CE2 . PHE   B 1 166 ? 28.179 -5.914  15.834  1.00 46.80  ? 859  PHE   B CE2 1 
ATOM   3529 C  CZ  . PHE   B 1 166 ? 29.258 -6.151  16.642  1.00 46.60  ? 859  PHE   B CZ  1 
ATOM   3530 N  N   . GLY   B 1 167 ? 28.345 -5.211  10.303  1.00 47.07  ? 860  GLY   B N   1 
ATOM   3531 C  CA  . GLY   B 1 167 ? 27.481 -4.068  10.030  1.00 47.84  ? 860  GLY   B CA  1 
ATOM   3532 C  C   . GLY   B 1 167 ? 28.187 -2.916  9.347   1.00 48.30  ? 860  GLY   B C   1 
ATOM   3533 O  O   . GLY   B 1 167 ? 27.529 -2.087  8.728   1.00 48.33  ? 860  GLY   B O   1 
ATOM   3534 N  N   . LEU   B 1 168 ? 29.530 -2.860  9.435   1.00 48.40  ? 861  LEU   B N   1 
ATOM   3535 C  CA  . LEU   B 1 168 ? 30.335 -1.820  8.811   1.00 48.98  ? 861  LEU   B CA  1 
ATOM   3536 C  C   . LEU   B 1 168 ? 30.212 -1.828  7.297   1.00 51.03  ? 861  LEU   B C   1 
ATOM   3537 O  O   . LEU   B 1 168 ? 30.081 -0.758  6.720   1.00 51.33  ? 861  LEU   B O   1 
ATOM   3538 C  CB  . LEU   B 1 168 ? 31.800 -1.942  9.224   1.00 48.41  ? 861  LEU   B CB  1 
ATOM   3539 C  CG  . LEU   B 1 168 ? 32.718 -0.866  8.680   1.00 49.33  ? 861  LEU   B CG  1 
ATOM   3540 C  CD1 . LEU   B 1 168 ? 32.326 0.502   9.193   1.00 49.83  ? 861  LEU   B CD1 1 
ATOM   3541 C  CD2 . LEU   B 1 168 ? 34.152 -1.166  8.999   1.00 49.91  ? 861  LEU   B CD2 1 
ATOM   3542 N  N   . ALA   B 1 169 ? 30.215 -3.007  6.645   1.00 52.60  ? 862  ALA   B N   1 
ATOM   3543 C  CA  . ALA   B 1 169 ? 30.064 -3.062  5.188   1.00 54.70  ? 862  ALA   B CA  1 
ATOM   3544 C  C   . ALA   B 1 169 ? 28.694 -2.535  4.757   1.00 56.46  ? 862  ALA   B C   1 
ATOM   3545 O  O   . ALA   B 1 169 ? 28.618 -1.785  3.795   1.00 56.93  ? 862  ALA   B O   1 
ATOM   3546 C  CB  . ALA   B 1 169 ? 30.283 -4.469  4.668   1.00 55.08  ? 862  ALA   B CB  1 
ATOM   3547 N  N   . LYS   B 1 170 ? 27.635 -2.863  5.494   1.00 57.50  ? 863  LYS   B N   1 
ATOM   3548 C  CA  . LYS   B 1 170 ? 26.300 -2.335  5.208   1.00 59.32  ? 863  LYS   B CA  1 
ATOM   3549 C  C   . LYS   B 1 170 ? 26.278 -0.823  5.503   1.00 60.45  ? 863  LYS   B C   1 
ATOM   3550 O  O   . LYS   B 1 170 ? 25.647 -0.070  4.772   1.00 60.98  ? 863  LYS   B O   1 
ATOM   3551 C  CB  . LYS   B 1 170 ? 25.254 -3.052  6.078   1.00 62.31  ? 863  LYS   B CB  1 
ATOM   3552 C  CG  . LYS   B 1 170 ? 23.858 -3.116  5.485   1.00 67.32  ? 863  LYS   B CG  1 
ATOM   3553 C  CD  . LYS   B 1 170 ? 22.824 -3.649  6.485   1.00 72.70  ? 863  LYS   B CD  1 
ATOM   3554 C  CE  . LYS   B 1 170 ? 21.422 -3.748  5.915   1.00 77.18  ? 863  LYS   B CE  1 
ATOM   3555 N  NZ  . LYS   B 1 170 ? 21.342 -4.687  4.754   1.00 79.87  ? 863  LYS   B NZ  1 
ATOM   3556 N  N   . LEU   B 1 171 ? 26.979 -0.389  6.560   1.00 60.89  ? 864  LEU   B N   1 
ATOM   3557 C  CA  . LEU   B 1 171 ? 27.115 0.998   6.986   1.00 62.12  ? 864  LEU   B CA  1 
ATOM   3558 C  C   . LEU   B 1 171 ? 27.662 1.859   5.849   1.00 63.25  ? 864  LEU   B C   1 
ATOM   3559 O  O   . LEU   B 1 171 ? 27.084 2.907   5.583   1.00 63.54  ? 864  LEU   B O   1 
ATOM   3560 C  CB  . LEU   B 1 171 ? 28.036 1.076   8.217   1.00 62.55  ? 864  LEU   B CB  1 
ATOM   3561 C  CG  . LEU   B 1 171 ? 27.868 2.237   9.194   1.00 64.29  ? 864  LEU   B CG  1 
ATOM   3562 C  CD1 . LEU   B 1 171 ? 28.414 3.521   8.635   1.00 64.89  ? 864  LEU   B CD1 1 
ATOM   3563 C  CD2 . LEU   B 1 171 ? 26.445 2.367   9.684   1.00 64.97  ? 864  LEU   B CD2 1 
ATOM   3564 N  N   . LEU   B 1 172 ? 28.748 1.431   5.163   1.00 63.64  ? 865  LEU   B N   1 
ATOM   3565 C  CA  . LEU   B 1 172 ? 29.288 2.231   4.061   1.00 64.42  ? 865  LEU   B CA  1 
ATOM   3566 C  C   . LEU   B 1 172 ? 28.837 1.724   2.673   1.00 65.85  ? 865  LEU   B C   1 
ATOM   3567 O  O   . LEU   B 1 172 ? 29.664 1.497   1.791   1.00 65.58  ? 865  LEU   B O   1 
ATOM   3568 C  CB  . LEU   B 1 172 ? 30.815 2.438   4.130   1.00 64.20  ? 865  LEU   B CB  1 
ATOM   3569 C  CG  . LEU   B 1 172 ? 31.696 1.328   4.689   1.00 65.07  ? 865  LEU   B CG  1 
ATOM   3570 C  CD1 . LEU   B 1 172 ? 32.195 0.430   3.582   1.00 65.64  ? 865  LEU   B CD1 1 
ATOM   3571 C  CD2 . LEU   B 1 172 ? 32.907 1.906   5.398   1.00 65.24  ? 865  LEU   B CD2 1 
ATOM   3572 N  N   . GLY   B 1 173 ? 27.516 1.607   2.507   1.00 67.21  ? 866  GLY   B N   1 
ATOM   3573 C  CA  . GLY   B 1 173 ? 26.846 1.201   1.277   1.00 68.99  ? 866  GLY   B CA  1 
ATOM   3574 C  C   . GLY   B 1 173 ? 27.278 -0.114  0.654   1.00 71.18  ? 866  GLY   B C   1 
ATOM   3575 O  O   . GLY   B 1 173 ? 28.331 -0.198  0.021   1.00 71.71  ? 866  GLY   B O   1 
ATOM   3576 N  N   . ALA   B 1 174 ? 26.473 -1.150  0.823   1.00 72.22  ? 867  ALA   B N   1 
ATOM   3577 C  CA  . ALA   B 1 174 ? 26.713 -2.468  0.216   1.00 73.80  ? 867  ALA   B CA  1 
ATOM   3578 C  C   . ALA   B 1 174 ? 25.371 -3.022  -0.301  1.00 75.18  ? 867  ALA   B C   1 
ATOM   3579 O  O   . ALA   B 1 174 ? 25.303 -3.612  -1.379  1.00 75.33  ? 867  ALA   B O   1 
ATOM   3580 C  CB  . ALA   B 1 174 ? 27.347 -3.426  1.213   1.00 73.89  ? 867  ALA   B CB  1 
ATOM   3581 N  N   . GLU   B 1 175 ? 24.304 -2.802  0.466   1.00 75.90  ? 868  GLU   B N   1 
ATOM   3582 C  CA  . GLU   B 1 175 ? 22.947 -3.145  0.086   1.00 77.33  ? 868  GLU   B CA  1 
ATOM   3583 C  C   . GLU   B 1 175 ? 22.399 -2.142  -0.949  1.00 78.59  ? 868  GLU   B C   1 
ATOM   3584 O  O   . GLU   B 1 175 ? 21.483 -2.489  -1.695  1.00 78.97  ? 868  GLU   B O   1 
ATOM   3585 C  CB  . GLU   B 1 175 ? 22.018 -3.180  1.315   1.00 80.01  ? 868  GLU   B CB  1 
ATOM   3586 C  CG  . GLU   B 1 175 ? 22.546 -2.523  2.586   1.00 84.41  ? 868  GLU   B CG  1 
ATOM   3587 C  CD  . GLU   B 1 175 ? 22.751 -1.018  2.608   1.00 88.85  ? 868  GLU   B CD  1 
ATOM   3588 O  OE1 . GLU   B 1 175 ? 23.843 -0.566  2.190   1.00 89.87  ? 868  GLU   B OE1 1 
ATOM   3589 O  OE2 . GLU   B 1 175 ? 21.829 -0.294  3.051   1.00 89.52  ? 868  GLU   B OE2 1 
ATOM   3590 N  N   . GLU   B 1 176 ? 22.926 -0.895  -0.980  1.00 79.06  ? 869  GLU   B N   1 
ATOM   3591 C  CA  . GLU   B 1 176 ? 22.473 0.116   -1.925  1.00 79.85  ? 869  GLU   B CA  1 
ATOM   3592 C  C   . GLU   B 1 176 ? 23.079 -0.210  -3.275  1.00 80.35  ? 869  GLU   B C   1 
ATOM   3593 O  O   . GLU   B 1 176 ? 24.302 -0.234  -3.422  1.00 80.15  ? 869  GLU   B O   1 
ATOM   3594 C  CB  . GLU   B 1 176 ? 22.863 1.537   -1.467  1.00 81.97  ? 869  GLU   B CB  1 
ATOM   3595 C  CG  . GLU   B 1 176 ? 22.523 1.850   -0.017  1.00 87.06  ? 869  GLU   B CG  1 
ATOM   3596 C  CD  . GLU   B 1 176 ? 21.053 1.987   0.351   1.00 94.46  ? 869  GLU   B CD  1 
ATOM   3597 O  OE1 . GLU   B 1 176 ? 20.205 2.099   -0.564  1.00 96.28  ? 869  GLU   B OE1 1 
ATOM   3598 O  OE2 . GLU   B 1 176 ? 20.750 1.993   1.567   1.00 96.64  ? 869  GLU   B OE2 1 
ATOM   3599 N  N   . LYS   B 1 177 ? 22.219 -0.538  -4.239  1.00 80.82  ? 870  LYS   B N   1 
ATOM   3600 C  CA  . LYS   B 1 177 ? 22.644 -0.898  -5.587  1.00 81.84  ? 870  LYS   B CA  1 
ATOM   3601 C  C   . LYS   B 1 177 ? 23.273 0.293   -6.316  1.00 82.42  ? 870  LYS   B C   1 
ATOM   3602 O  O   . LYS   B 1 177 ? 24.203 0.112   -7.103  1.00 82.39  ? 870  LYS   B O   1 
ATOM   3603 C  CB  . LYS   B 1 177 ? 21.465 -1.470  -6.392  1.00 84.06  ? 870  LYS   B CB  1 
ATOM   3604 C  CG  . LYS   B 1 177 ? 21.196 -2.951  -6.137  1.00 88.63  ? 870  LYS   B CG  1 
ATOM   3605 C  CD  . LYS   B 1 177 ? 20.309 -3.184  -4.921  1.00 93.45  ? 870  LYS   B CD  1 
ATOM   3606 C  CE  . LYS   B 1 177 ? 20.344 -4.624  -4.475  1.00 97.28  ? 870  LYS   B CE  1 
ATOM   3607 N  NZ  . LYS   B 1 177 ? 19.636 -4.808  -3.182  1.00 99.55  ? 870  LYS   B NZ  1 
ATOM   3608 N  N   . GLU   B 1 178 ? 22.775 1.511   -6.033  1.00 82.70  ? 871  GLU   B N   1 
ATOM   3609 C  CA  . GLU   B 1 178 ? 23.276 2.740   -6.626  1.00 83.41  ? 871  GLU   B CA  1 
ATOM   3610 C  C   . GLU   B 1 178 ? 24.715 3.045   -6.176  1.00 84.05  ? 871  GLU   B C   1 
ATOM   3611 O  O   . GLU   B 1 178 ? 25.482 3.624   -6.949  1.00 84.17  ? 871  GLU   B O   1 
ATOM   3612 C  CB  . GLU   B 1 178 ? 22.352 3.920   -6.275  1.00 85.32  ? 871  GLU   B CB  1 
ATOM   3613 C  CG  . GLU   B 1 178 ? 20.942 3.835   -6.838  1.00 89.36  ? 871  GLU   B CG  1 
ATOM   3614 C  CD  . GLU   B 1 178 ? 20.084 5.069   -6.608  1.00 94.30  ? 871  GLU   B CD  1 
ATOM   3615 O  OE1 . GLU   B 1 178 ? 20.603 6.070   -6.061  1.00 94.64  ? 871  GLU   B OE1 1 
ATOM   3616 O  OE2 . GLU   B 1 178 ? 18.887 5.034   -6.976  1.00 96.04  ? 871  GLU   B OE2 1 
ATOM   3617 N  N   . TYR   B 1 179 ? 25.081 2.676   -4.932  1.00 84.22  ? 872  TYR   B N   1 
ATOM   3618 C  CA  . TYR   B 1 179 ? 26.423 2.969   -4.434  1.00 84.93  ? 872  TYR   B CA  1 
ATOM   3619 C  C   . TYR   B 1 179 ? 27.440 1.934   -4.820  1.00 85.34  ? 872  TYR   B C   1 
ATOM   3620 O  O   . TYR   B 1 179 ? 27.355 0.789   -4.369  1.00 85.43  ? 872  TYR   B O   1 
ATOM   3621 C  CB  . TYR   B 1 179 ? 26.450 3.215   -2.914  1.00 85.23  ? 872  TYR   B CB  1 
ATOM   3622 C  CG  . TYR   B 1 179 ? 27.824 3.622   -2.415  1.00 86.32  ? 872  TYR   B CG  1 
ATOM   3623 C  CD1 . TYR   B 1 179 ? 28.410 4.813   -2.825  1.00 87.33  ? 872  TYR   B CD1 1 
ATOM   3624 C  CD2 . TYR   B 1 179 ? 28.543 2.808   -1.554  1.00 87.25  ? 872  TYR   B CD2 1 
ATOM   3625 C  CE1 . TYR   B 1 179 ? 29.679 5.179   -2.393  1.00 88.30  ? 872  TYR   B CE1 1 
ATOM   3626 C  CE2 . TYR   B 1 179 ? 29.810 3.167   -1.109  1.00 88.24  ? 872  TYR   B CE2 1 
ATOM   3627 C  CZ  . TYR   B 1 179 ? 30.376 4.353   -1.532  1.00 89.26  ? 872  TYR   B CZ  1 
ATOM   3628 O  OH  . TYR   B 1 179 ? 31.633 4.703   -1.097  1.00 90.92  ? 872  TYR   B OH  1 
ATOM   3629 N  N   . HIS   B 1 180 ? 28.441 2.345   -5.615  1.00 85.56  ? 873  HIS   B N   1 
ATOM   3630 C  CA  . HIS   B 1 180 ? 29.500 1.413   -5.999  1.00 86.20  ? 873  HIS   B CA  1 
ATOM   3631 C  C   . HIS   B 1 180 ? 30.841 2.111   -6.229  1.00 86.37  ? 873  HIS   B C   1 
ATOM   3632 O  O   . HIS   B 1 180 ? 31.577 1.730   -7.140  1.00 86.85  ? 873  HIS   B O   1 
ATOM   3633 C  CB  . HIS   B 1 180 ? 29.103 0.525   -7.201  1.00 87.21  ? 873  HIS   B CB  1 
ATOM   3634 C  CG  . HIS   B 1 180 ? 28.191 1.188   -8.194  1.00 89.27  ? 873  HIS   B CG  1 
ATOM   3635 N  ND1 . HIS   B 1 180 ? 28.567 2.338   -8.860  1.00 91.10  ? 873  HIS   B ND1 1 
ATOM   3636 C  CD2 . HIS   B 1 180 ? 26.942 0.843   -8.586  1.00 90.29  ? 873  HIS   B CD2 1 
ATOM   3637 C  CE1 . HIS   B 1 180 ? 27.542 2.654   -9.634  1.00 91.64  ? 873  HIS   B CE1 1 
ATOM   3638 N  NE2 . HIS   B 1 180 ? 26.541 1.785   -9.500  1.00 91.43  ? 873  HIS   B NE2 1 
ATOM   3639 N  N   . ALA   B 1 181 ? 31.171 3.112   -5.387  1.00 85.62  ? 874  ALA   B N   1 
ATOM   3640 C  CA  . ALA   B 1 181 ? 32.428 3.856   -5.479  1.00 85.27  ? 874  ALA   B CA  1 
ATOM   3641 C  C   . ALA   B 1 181 ? 33.526 3.176   -4.643  1.00 84.62  ? 874  ALA   B C   1 
ATOM   3642 O  O   . ALA   B 1 181 ? 34.253 3.832   -3.895  1.00 84.87  ? 874  ALA   B O   1 
ATOM   3643 C  CB  . ALA   B 1 181 ? 32.215 5.293   -5.019  1.00 85.44  ? 874  ALA   B CB  1 
ATOM   3644 N  N   . GLU   B 1 182 ? 33.642 1.851   -4.782  1.00 83.59  ? 875  GLU   B N   1 
ATOM   3645 C  CA  . GLU   B 1 182 ? 34.616 1.045   -4.053  1.00 83.19  ? 875  GLU   B CA  1 
ATOM   3646 C  C   . GLU   B 1 182 ? 35.605 0.417   -5.048  1.00 81.43  ? 875  GLU   B C   1 
ATOM   3647 O  O   . GLU   B 1 182 ? 35.334 -0.649  -5.603  1.00 81.56  ? 875  GLU   B O   1 
ATOM   3648 C  CB  . GLU   B 1 182 ? 33.889 -0.060  -3.251  1.00 86.73  ? 875  GLU   B CB  1 
ATOM   3649 C  CG  . GLU   B 1 182 ? 32.650 0.391   -2.486  1.00 93.13  ? 875  GLU   B CG  1 
ATOM   3650 C  CD  . GLU   B 1 182 ? 31.325 -0.177  -2.972  1.00 101.15 ? 875  GLU   B CD  1 
ATOM   3651 O  OE1 . GLU   B 1 182 ? 31.303 -0.847  -4.031  1.00 103.39 ? 875  GLU   B OE1 1 
ATOM   3652 O  OE2 . GLU   B 1 182 ? 30.302 0.047   -2.288  1.00 103.26 ? 875  GLU   B OE2 1 
ATOM   3653 N  N   . GLY   B 1 183 ? 36.722 1.092   -5.285  1.00 79.62  ? 876  GLY   B N   1 
ATOM   3654 C  CA  . GLY   B 1 183 ? 37.725 0.628   -6.240  1.00 78.18  ? 876  GLY   B CA  1 
ATOM   3655 C  C   . GLY   B 1 183 ? 38.543 -0.556  -5.769  1.00 76.17  ? 876  GLY   B C   1 
ATOM   3656 O  O   . GLY   B 1 183 ? 38.158 -1.711  -5.965  1.00 76.28  ? 876  GLY   B O   1 
ATOM   3657 N  N   . GLY   B 1 184 ? 39.683 -0.265  -5.159  1.00 74.11  ? 877  GLY   B N   1 
ATOM   3658 C  CA  . GLY   B 1 184 ? 40.553 -1.300  -4.611  1.00 72.47  ? 877  GLY   B CA  1 
ATOM   3659 C  C   . GLY   B 1 184 ? 40.262 -1.634  -3.156  1.00 70.27  ? 877  GLY   B C   1 
ATOM   3660 O  O   . GLY   B 1 184 ? 41.043 -2.342  -2.512  1.00 70.44  ? 877  GLY   B O   1 
ATOM   3661 N  N   . LYS   B 1 185 ? 39.123 -1.125  -2.625  1.00 67.88  ? 878  LYS   B N   1 
ATOM   3662 C  CA  . LYS   B 1 185 ? 38.687 -1.337  -1.243  1.00 65.92  ? 878  LYS   B CA  1 
ATOM   3663 C  C   . LYS   B 1 185 ? 37.773 -2.570  -1.063  1.00 63.18  ? 878  LYS   B C   1 
ATOM   3664 O  O   . LYS   B 1 185 ? 37.281 -2.810  0.039   1.00 63.19  ? 878  LYS   B O   1 
ATOM   3665 C  CB  . LYS   B 1 185 ? 37.981 -0.075  -0.690  1.00 67.82  ? 878  LYS   B CB  1 
ATOM   3666 C  CG  . LYS   B 1 185 ? 38.704 1.243   -0.958  1.00 71.70  ? 878  LYS   B CG  1 
ATOM   3667 C  CD  . LYS   B 1 185 ? 37.899 2.108   -1.926  1.00 76.65  ? 878  LYS   B CD  1 
ATOM   3668 C  CE  . LYS   B 1 185 ? 38.765 2.945   -2.849  1.00 80.46  ? 878  LYS   B CE  1 
ATOM   3669 N  NZ  . LYS   B 1 185 ? 37.952 3.631   -3.895  1.00 82.23  ? 878  LYS   B NZ  1 
ATOM   3670 N  N   . VAL   B 1 186 ? 37.527 -3.334  -2.130  1.00 60.59  ? 879  VAL   B N   1 
ATOM   3671 C  CA  . VAL   B 1 186 ? 36.671 -4.515  -2.067  1.00 58.54  ? 879  VAL   B CA  1 
ATOM   3672 C  C   . VAL   B 1 186 ? 37.511 -5.805  -1.828  1.00 55.40  ? 879  VAL   B C   1 
ATOM   3673 O  O   . VAL   B 1 186 ? 38.543 -6.010  -2.475  1.00 55.30  ? 879  VAL   B O   1 
ATOM   3674 C  CB  . VAL   B 1 186 ? 35.730 -4.580  -3.301  1.00 59.58  ? 879  VAL   B CB  1 
ATOM   3675 C  CG1 . VAL   B 1 186 ? 36.487 -4.339  -4.607  1.00 60.55  ? 879  VAL   B CG1 1 
ATOM   3676 C  CG2 . VAL   B 1 186 ? 34.934 -5.877  -3.343  1.00 59.85  ? 879  VAL   B CG2 1 
ATOM   3677 N  N   . PRO   B 1 187 ? 37.126 -6.631  -0.823  1.00 52.55  ? 880  PRO   B N   1 
ATOM   3678 C  CA  . PRO   B 1 187 ? 37.929 -7.827  -0.495  1.00 50.67  ? 880  PRO   B CA  1 
ATOM   3679 C  C   . PRO   B 1 187 ? 37.658 -9.069  -1.346  1.00 48.65  ? 880  PRO   B C   1 
ATOM   3680 O  O   . PRO   B 1 187 ? 37.168 -10.076 -0.844  1.00 49.10  ? 880  PRO   B O   1 
ATOM   3681 C  CB  . PRO   B 1 187 ? 37.596 -8.070  0.978   1.00 51.24  ? 880  PRO   B CB  1 
ATOM   3682 C  CG  . PRO   B 1 187 ? 36.218 -7.529  1.139   1.00 51.93  ? 880  PRO   B CG  1 
ATOM   3683 C  CD  . PRO   B 1 187 ? 35.973 -6.480  0.087   1.00 51.14  ? 880  PRO   B CD  1 
ATOM   3684 N  N   . ILE   B 1 188 ? 38.027 -9.007  -2.616  1.00 46.37  ? 881  ILE   B N   1 
ATOM   3685 C  CA  . ILE   B 1 188 ? 37.835 -10.055 -3.608  1.00 44.96  ? 881  ILE   B CA  1 
ATOM   3686 C  C   . ILE   B 1 188 ? 38.454 -11.437 -3.227  1.00 43.71  ? 881  ILE   B C   1 
ATOM   3687 O  O   . ILE   B 1 188 ? 37.857 -12.480 -3.514  1.00 43.93  ? 881  ILE   B O   1 
ATOM   3688 C  CB  . ILE   B 1 188 ? 38.393 -9.499  -4.943  1.00 45.11  ? 881  ILE   B CB  1 
ATOM   3689 C  CG1 . ILE   B 1 188 ? 37.540 -8.320  -5.447  1.00 45.75  ? 881  ILE   B CG1 1 
ATOM   3690 C  CG2 . ILE   B 1 188 ? 38.539 -10.568 -5.999  1.00 45.26  ? 881  ILE   B CG2 1 
ATOM   3691 C  CD1 . ILE   B 1 188 ? 36.075 -8.655  -5.724  1.00 46.81  ? 881  ILE   B CD1 1 
ATOM   3692 N  N   . LYS   B 1 189 ? 39.616 -11.441 -2.550  1.00 42.15  ? 882  LYS   B N   1 
ATOM   3693 C  CA  . LYS   B 1 189 ? 40.303 -12.674 -2.157  1.00 41.27  ? 882  LYS   B CA  1 
ATOM   3694 C  C   . LYS   B 1 189 ? 39.698 -13.387 -0.931  1.00 41.11  ? 882  LYS   B C   1 
ATOM   3695 O  O   . LYS   B 1 189 ? 40.183 -14.458 -0.545  1.00 41.12  ? 882  LYS   B O   1 
ATOM   3696 C  CB  . LYS   B 1 189 ? 41.796 -12.431 -1.974  1.00 42.35  ? 882  LYS   B CB  1 
ATOM   3697 C  CG  . LYS   B 1 189 ? 42.420 -11.953 -3.266  1.00 46.37  ? 882  LYS   B CG  1 
ATOM   3698 C  CD  . LYS   B 1 189 ? 43.897 -11.686 -3.156  1.00 50.93  ? 882  LYS   B CD  1 
ATOM   3699 C  CE  . LYS   B 1 189 ? 44.465 -11.276 -4.481  1.00 55.54  ? 882  LYS   B CE  1 
ATOM   3700 N  NZ  . LYS   B 1 189 ? 45.950 -11.205 -4.444  1.00 58.42  ? 882  LYS   B NZ  1 
ATOM   3701 N  N   . TRP   B 1 190 ? 38.630 -12.809 -0.350  1.00 40.56  ? 883  TRP   B N   1 
ATOM   3702 C  CA  . TRP   B 1 190 ? 37.860 -13.366 0.757   1.00 40.82  ? 883  TRP   B CA  1 
ATOM   3703 C  C   . TRP   B 1 190 ? 36.382 -13.560 0.362   1.00 41.83  ? 883  TRP   B C   1 
ATOM   3704 O  O   . TRP   B 1 190 ? 35.619 -14.113 1.151   1.00 42.81  ? 883  TRP   B O   1 
ATOM   3705 C  CB  . TRP   B 1 190 ? 37.925 -12.443 1.990   1.00 40.11  ? 883  TRP   B CB  1 
ATOM   3706 C  CG  . TRP   B 1 190 ? 39.189 -12.558 2.777   1.00 39.42  ? 883  TRP   B CG  1 
ATOM   3707 C  CD1 . TRP   B 1 190 ? 39.388 -13.288 3.909   1.00 40.04  ? 883  TRP   B CD1 1 
ATOM   3708 C  CD2 . TRP   B 1 190 ? 40.436 -11.930 2.480   1.00 39.25  ? 883  TRP   B CD2 1 
ATOM   3709 N  NE1 . TRP   B 1 190 ? 40.689 -13.161 4.331   1.00 40.23  ? 883  TRP   B NE1 1 
ATOM   3710 C  CE2 . TRP   B 1 190 ? 41.357 -12.334 3.468   1.00 39.94  ? 883  TRP   B CE2 1 
ATOM   3711 C  CE3 . TRP   B 1 190 ? 40.858 -11.032 1.493   1.00 39.79  ? 883  TRP   B CE3 1 
ATOM   3712 C  CZ2 . TRP   B 1 190 ? 42.674 -11.881 3.491   1.00 40.66  ? 883  TRP   B CZ2 1 
ATOM   3713 C  CZ3 . TRP   B 1 190 ? 42.169 -10.606 1.503   1.00 40.63  ? 883  TRP   B CZ3 1 
ATOM   3714 C  CH2 . TRP   B 1 190 ? 43.058 -11.014 2.501   1.00 40.82  ? 883  TRP   B CH2 1 
ATOM   3715 N  N   . MET   B 1 191 ? 35.963 -13.078 -0.816  1.00 41.48  ? 884  MET   B N   1 
ATOM   3716 C  CA  . MET   B 1 191 ? 34.585 -13.156 -1.260  1.00 41.87  ? 884  MET   B CA  1 
ATOM   3717 C  C   . MET   B 1 191 ? 34.247 -14.414 -2.019  1.00 41.72  ? 884  MET   B C   1 
ATOM   3718 O  O   . MET   B 1 191 ? 35.055 -14.929 -2.804  1.00 41.74  ? 884  MET   B O   1 
ATOM   3719 C  CB  . MET   B 1 191 ? 34.246 -11.949 -2.139  1.00 42.73  ? 884  MET   B CB  1 
ATOM   3720 C  CG  . MET   B 1 191 ? 34.037 -10.683 -1.361  1.00 45.36  ? 884  MET   B CG  1 
ATOM   3721 S  SD  . MET   B 1 191 ? 34.292 -9.223  -2.388  1.00 50.65  ? 884  MET   B SD  1 
ATOM   3722 C  CE  . MET   B 1 191 ? 32.914 -9.344  -3.454  1.00 48.68  ? 884  MET   B CE  1 
ATOM   3723 N  N   . ALA   B 1 192 ? 33.011 -14.868 -1.823  1.00 41.38  ? 885  ALA   B N   1 
ATOM   3724 C  CA  . ALA   B 1 192 ? 32.470 -16.008 -2.536  1.00 41.77  ? 885  ALA   B CA  1 
ATOM   3725 C  C   . ALA   B 1 192 ? 32.210 -15.599 -3.984  1.00 42.15  ? 885  ALA   B C   1 
ATOM   3726 O  O   . ALA   B 1 192 ? 31.988 -14.418 -4.256  1.00 42.56  ? 885  ALA   B O   1 
ATOM   3727 C  CB  . ALA   B 1 192 ? 31.178 -16.456 -1.878  1.00 41.93  ? 885  ALA   B CB  1 
ATOM   3728 N  N   . LEU   B 1 193 ? 32.223 -16.554 -4.917  1.00 42.10  ? 886  LEU   B N   1 
ATOM   3729 C  CA  . LEU   B 1 193 ? 32.005 -16.256 -6.335  1.00 42.56  ? 886  LEU   B CA  1 
ATOM   3730 C  C   . LEU   B 1 193 ? 30.716 -15.481 -6.610  1.00 42.77  ? 886  LEU   B C   1 
ATOM   3731 O  O   . LEU   B 1 193 ? 30.757 -14.491 -7.333  1.00 43.47  ? 886  LEU   B O   1 
ATOM   3732 C  CB  . LEU   B 1 193 ? 32.067 -17.535 -7.182  1.00 42.98  ? 886  LEU   B CB  1 
ATOM   3733 C  CG  . LEU   B 1 193 ? 32.172 -17.353 -8.688  1.00 43.90  ? 886  LEU   B CG  1 
ATOM   3734 C  CD1 . LEU   B 1 193 ? 33.418 -16.587 -9.058  1.00 44.31  ? 886  LEU   B CD1 1 
ATOM   3735 C  CD2 . LEU   B 1 193 ? 32.183 -18.688 -9.373  1.00 44.13  ? 886  LEU   B CD2 1 
ATOM   3736 N  N   . GLU   B 1 194 ? 29.600 -15.871 -5.995  1.00 42.47  ? 887  GLU   B N   1 
ATOM   3737 C  CA  . GLU   B 1 194 ? 28.337 -15.153 -6.179  1.00 43.41  ? 887  GLU   B CA  1 
ATOM   3738 C  C   . GLU   B 1 194 ? 28.372 -13.706 -5.669  1.00 44.62  ? 887  GLU   B C   1 
ATOM   3739 O  O   . GLU   B 1 194 ? 27.487 -12.925 -6.005  1.00 45.13  ? 887  GLU   B O   1 
ATOM   3740 C  CB  . GLU   B 1 194 ? 27.165 -15.917 -5.538  1.00 44.97  ? 887  GLU   B CB  1 
ATOM   3741 C  CG  . GLU   B 1 194 ? 27.157 -15.895 -4.017  1.00 47.40  ? 887  GLU   B CG  1 
ATOM   3742 C  CD  . GLU   B 1 194 ? 27.918 -17.011 -3.332  1.00 50.36  ? 887  GLU   B CD  1 
ATOM   3743 O  OE1 . GLU   B 1 194 ? 28.741 -17.692 -3.989  1.00 51.69  ? 887  GLU   B OE1 1 
ATOM   3744 O  OE2 . GLU   B 1 194 ? 27.683 -17.202 -2.120  1.00 50.53  ? 887  GLU   B OE2 1 
ATOM   3745 N  N   . SER   B 1 195 ? 29.357 -13.359 -4.832  1.00 45.00  ? 888  SER   B N   1 
ATOM   3746 C  CA  . SER   B 1 195 ? 29.508 -12.011 -4.311  1.00 45.93  ? 888  SER   B CA  1 
ATOM   3747 C  C   . SER   B 1 195 ? 30.373 -11.188 -5.271  1.00 47.12  ? 888  SER   B C   1 
ATOM   3748 O  O   . SER   B 1 195 ? 30.087 -10.010 -5.486  1.00 47.41  ? 888  SER   B O   1 
ATOM   3749 C  CB  . SER   B 1 195 ? 30.128 -12.037 -2.921  1.00 46.72  ? 888  SER   B CB  1 
ATOM   3750 O  OG  . SER   B 1 195 ? 29.295 -12.727 -2.007  1.00 48.58  ? 888  SER   B OG  1 
ATOM   3751 N  N   . ILE   B 1 196 ? 31.424 -11.805 -5.846  1.00 47.24  ? 889  ILE   B N   1 
ATOM   3752 C  CA  . ILE   B 1 196 ? 32.301 -11.156 -6.813  1.00 47.86  ? 889  ILE   B CA  1 
ATOM   3753 C  C   . ILE   B 1 196 ? 31.499 -10.869 -8.087  1.00 49.39  ? 889  ILE   B C   1 
ATOM   3754 O  O   . ILE   B 1 196 ? 31.554 -9.765  -8.628  1.00 49.63  ? 889  ILE   B O   1 
ATOM   3755 C  CB  . ILE   B 1 196 ? 33.535 -12.055 -7.129  1.00 47.53  ? 889  ILE   B CB  1 
ATOM   3756 C  CG1 . ILE   B 1 196 ? 34.446 -12.233 -5.913  1.00 47.83  ? 889  ILE   B CG1 1 
ATOM   3757 C  CG2 . ILE   B 1 196 ? 34.314 -11.525 -8.332  1.00 47.63  ? 889  ILE   B CG2 1 
ATOM   3758 C  CD1 . ILE   B 1 196 ? 35.493 -13.306 -6.098  1.00 48.71  ? 889  ILE   B CD1 1 
ATOM   3759 N  N   . LEU   B 1 197 ? 30.737 -11.859 -8.551  1.00 50.27  ? 890  LEU   B N   1 
ATOM   3760 C  CA  . LEU   B 1 197 ? 29.967 -11.725 -9.774  1.00 51.20  ? 890  LEU   B CA  1 
ATOM   3761 C  C   . LEU   B 1 197 ? 28.687 -10.926 -9.638  1.00 52.22  ? 890  LEU   B C   1 
ATOM   3762 O  O   . LEU   B 1 197 ? 28.437 -10.066 -10.482 1.00 52.72  ? 890  LEU   B O   1 
ATOM   3763 C  CB  . LEU   B 1 197 ? 29.643 -13.101 -10.379 1.00 51.30  ? 890  LEU   B CB  1 
ATOM   3764 C  CG  . LEU   B 1 197 ? 30.810 -14.016 -10.708 1.00 53.23  ? 890  LEU   B CG  1 
ATOM   3765 C  CD1 . LEU   B 1 197 ? 30.319 -15.260 -11.388 1.00 53.97  ? 890  LEU   B CD1 1 
ATOM   3766 C  CD2 . LEU   B 1 197 ? 31.826 -13.330 -11.609 1.00 54.23  ? 890  LEU   B CD2 1 
ATOM   3767 N  N   . HIS   B 1 198 ? 27.853 -11.218 -8.622  1.00 52.28  ? 891  HIS   B N   1 
ATOM   3768 C  CA  . HIS   B 1 198 ? 26.538 -10.593 -8.554  1.00 53.00  ? 891  HIS   B CA  1 
ATOM   3769 C  C   . HIS   B 1 198 ? 26.243 -9.792  -7.310  1.00 53.19  ? 891  HIS   B C   1 
ATOM   3770 O  O   . HIS   B 1 198 ? 25.081 -9.437  -7.102  1.00 53.24  ? 891  HIS   B O   1 
ATOM   3771 C  CB  . HIS   B 1 198 ? 25.449 -11.658 -8.754  1.00 54.42  ? 891  HIS   B CB  1 
ATOM   3772 C  CG  . HIS   B 1 198 ? 25.694 -12.519 -9.948  1.00 57.78  ? 891  HIS   B CG  1 
ATOM   3773 N  ND1 . HIS   B 1 198 ? 26.088 -13.841 -9.815  1.00 60.20  ? 891  HIS   B ND1 1 
ATOM   3774 C  CD2 . HIS   B 1 198 ? 25.714 -12.187 -11.260 1.00 59.29  ? 891  HIS   B CD2 1 
ATOM   3775 C  CE1 . HIS   B 1 198 ? 26.273 -14.290 -11.049 1.00 60.78  ? 891  HIS   B CE1 1 
ATOM   3776 N  NE2 . HIS   B 1 198 ? 26.067 -13.329 -11.953 1.00 60.69  ? 891  HIS   B NE2 1 
ATOM   3777 N  N   . ARG   B 1 199 ? 27.261 -9.490  -6.492  1.00 53.32  ? 892  ARG   B N   1 
ATOM   3778 C  CA  . ARG   B 1 199 ? 27.088 -8.722  -5.256  1.00 53.90  ? 892  ARG   B CA  1 
ATOM   3779 C  C   . ARG   B 1 199 ? 26.003 -9.309  -4.338  1.00 52.81  ? 892  ARG   B C   1 
ATOM   3780 O  O   . ARG   B 1 199 ? 25.226 -8.564  -3.729  1.00 52.98  ? 892  ARG   B O   1 
ATOM   3781 C  CB  . ARG   B 1 199 ? 26.850 -7.226  -5.541  1.00 56.82  ? 892  ARG   B CB  1 
ATOM   3782 C  CG  . ARG   B 1 199 ? 28.099 -6.469  -5.995  1.00 63.62  ? 892  ARG   B CG  1 
ATOM   3783 C  CD  . ARG   B 1 199 ? 29.174 -6.439  -4.910  1.00 70.40  ? 892  ARG   B CD  1 
ATOM   3784 N  NE  . ARG   B 1 199 ? 30.376 -5.685  -5.292  1.00 75.71  ? 892  ARG   B NE  1 
ATOM   3785 C  CZ  . ARG   B 1 199 ? 31.421 -6.210  -5.931  1.00 79.54  ? 892  ARG   B CZ  1 
ATOM   3786 N  NH1 . ARG   B 1 199 ? 31.414 -7.490  -6.294  1.00 79.50  ? 892  ARG   B NH1 1 
ATOM   3787 N  NH2 . ARG   B 1 199 ? 32.472 -5.455  -6.228  1.00 80.19  ? 892  ARG   B NH2 1 
ATOM   3788 N  N   . ILE   B 1 200 ? 25.940 -10.654 -4.275  1.00 51.41  ? 893  ILE   B N   1 
ATOM   3789 C  CA  . ILE   B 1 200 ? 24.997 -11.393 -3.433  1.00 50.72  ? 893  ILE   B CA  1 
ATOM   3790 C  C   . ILE   B 1 200 ? 25.702 -11.741 -2.121  1.00 49.48  ? 893  ILE   B C   1 
ATOM   3791 O  O   . ILE   B 1 200 ? 26.741 -12.405 -2.144  1.00 49.53  ? 893  ILE   B O   1 
ATOM   3792 C  CB  . ILE   B 1 200 ? 24.502 -12.677 -4.150  1.00 51.12  ? 893  ILE   B CB  1 
ATOM   3793 C  CG1 . ILE   B 1 200 ? 23.702 -12.339 -5.409  1.00 51.87  ? 893  ILE   B CG1 1 
ATOM   3794 C  CG2 . ILE   B 1 200 ? 23.688 -13.568 -3.201  1.00 51.57  ? 893  ILE   B CG2 1 
ATOM   3795 C  CD1 . ILE   B 1 200 ? 23.467 -13.520 -6.286  1.00 53.16  ? 893  ILE   B CD1 1 
ATOM   3796 N  N   . TYR   B 1 201 ? 25.143 -11.297 -0.987  1.00 48.11  ? 894  TYR   B N   1 
ATOM   3797 C  CA  . TYR   B 1 201 ? 25.731 -11.543 0.330   1.00 47.16  ? 894  TYR   B CA  1 
ATOM   3798 C  C   . TYR   B 1 201 ? 24.794 -12.300 1.243   1.00 46.23  ? 894  TYR   B C   1 
ATOM   3799 O  O   . TYR   B 1 201 ? 23.750 -11.786 1.631   1.00 46.51  ? 894  TYR   B O   1 
ATOM   3800 C  CB  . TYR   B 1 201 ? 26.154 -10.226 0.991   1.00 46.71  ? 894  TYR   B CB  1 
ATOM   3801 C  CG  . TYR   B 1 201 ? 27.237 -9.516  0.218   1.00 46.96  ? 894  TYR   B CG  1 
ATOM   3802 C  CD1 . TYR   B 1 201 ? 28.570 -9.846  0.393   1.00 47.63  ? 894  TYR   B CD1 1 
ATOM   3803 C  CD2 . TYR   B 1 201 ? 26.924 -8.550  -0.724  1.00 47.83  ? 894  TYR   B CD2 1 
ATOM   3804 C  CE1 . TYR   B 1 201 ? 29.568 -9.218  -0.334  1.00 48.51  ? 894  TYR   B CE1 1 
ATOM   3805 C  CE2 . TYR   B 1 201 ? 27.915 -7.919  -1.464  1.00 48.61  ? 894  TYR   B CE2 1 
ATOM   3806 C  CZ  . TYR   B 1 201 ? 29.239 -8.246  -1.256  1.00 49.47  ? 894  TYR   B CZ  1 
ATOM   3807 O  OH  . TYR   B 1 201 ? 30.230 -7.621  -1.968  1.00 51.12  ? 894  TYR   B OH  1 
ATOM   3808 N  N   . THR   B 1 202 ? 25.148 -13.530 1.567   1.00 45.17  ? 895  THR   B N   1 
ATOM   3809 C  CA  . THR   B 1 202 ? 24.346 -14.355 2.465   1.00 45.02  ? 895  THR   B CA  1 
ATOM   3810 C  C   . THR   B 1 202 ? 25.231 -14.921 3.603   1.00 43.86  ? 895  THR   B C   1 
ATOM   3811 O  O   . THR   B 1 202 ? 26.456 -14.749 3.574   1.00 44.17  ? 895  THR   B O   1 
ATOM   3812 C  CB  . THR   B 1 202 ? 23.661 -15.485 1.667   1.00 46.93  ? 895  THR   B CB  1 
ATOM   3813 O  OG1 . THR   B 1 202 ? 24.647 -16.420 1.239   1.00 48.08  ? 895  THR   B OG1 1 
ATOM   3814 C  CG2 . THR   B 1 202 ? 22.854 -14.981 0.492   1.00 47.83  ? 895  THR   B CG2 1 
ATOM   3815 N  N   . HIS   B 1 203 ? 24.630 -15.626 4.587   1.00 42.17  ? 896  HIS   B N   1 
ATOM   3816 C  CA  . HIS   B 1 203 ? 25.409 -16.293 5.624   1.00 41.10  ? 896  HIS   B CA  1 
ATOM   3817 C  C   . HIS   B 1 203 ? 26.355 -17.341 5.016   1.00 40.65  ? 896  HIS   B C   1 
ATOM   3818 O  O   . HIS   B 1 203 ? 27.425 -17.578 5.560   1.00 40.66  ? 896  HIS   B O   1 
ATOM   3819 C  CB  . HIS   B 1 203 ? 24.474 -16.958 6.635   1.00 40.94  ? 896  HIS   B CB  1 
ATOM   3820 C  CG  . HIS   B 1 203 ? 23.611 -15.978 7.356   1.00 40.99  ? 896  HIS   B CG  1 
ATOM   3821 N  ND1 . HIS   B 1 203 ? 22.240 -16.010 7.242   1.00 42.37  ? 896  HIS   B ND1 1 
ATOM   3822 C  CD2 . HIS   B 1 203 ? 23.960 -14.940 8.150   1.00 41.48  ? 896  HIS   B CD2 1 
ATOM   3823 C  CE1 . HIS   B 1 203 ? 21.795 -15.009 7.987   1.00 42.78  ? 896  HIS   B CE1 1 
ATOM   3824 N  NE2 . HIS   B 1 203 ? 22.797 -14.333 8.546   1.00 42.61  ? 896  HIS   B NE2 1 
ATOM   3825 N  N   . GLN   B 1 204 ? 25.977 -17.929 3.863   1.00 40.08  ? 897  GLN   B N   1 
ATOM   3826 C  CA  . GLN   B 1 204 ? 26.780 -18.918 3.158   1.00 39.79  ? 897  GLN   B CA  1 
ATOM   3827 C  C   . GLN   B 1 204 ? 27.959 -18.303 2.431   1.00 39.10  ? 897  GLN   B C   1 
ATOM   3828 O  O   . GLN   B 1 204 ? 28.984 -18.962 2.277   1.00 39.07  ? 897  GLN   B O   1 
ATOM   3829 C  CB  . GLN   B 1 204 ? 25.902 -19.769 2.247   1.00 41.34  ? 897  GLN   B CB  1 
ATOM   3830 C  CG  . GLN   B 1 204 ? 24.840 -20.553 3.045   1.00 44.43  ? 897  GLN   B CG  1 
ATOM   3831 C  CD  . GLN   B 1 204 ? 25.411 -21.405 4.163   1.00 47.23  ? 897  GLN   B CD  1 
ATOM   3832 O  OE1 . GLN   B 1 204 ? 26.172 -22.353 3.923   1.00 48.86  ? 897  GLN   B OE1 1 
ATOM   3833 N  NE2 . GLN   B 1 204 ? 25.051 -21.082 5.405   1.00 46.85  ? 897  GLN   B NE2 1 
ATOM   3834 N  N   . SER   B 1 205 ? 27.850 -17.026 2.032   1.00 38.42  ? 898  SER   B N   1 
ATOM   3835 C  CA  . SER   B 1 205 ? 28.993 -16.295 1.482   1.00 37.73  ? 898  SER   B CA  1 
ATOM   3836 C  C   . SER   B 1 205 ? 29.975 -15.976 2.657   1.00 36.52  ? 898  SER   B C   1 
ATOM   3837 O  O   . SER   B 1 205 ? 31.189 -15.979 2.464   1.00 36.39  ? 898  SER   B O   1 
ATOM   3838 C  CB  . SER   B 1 205 ? 28.543 -15.023 0.771   1.00 38.86  ? 898  SER   B CB  1 
ATOM   3839 O  OG  . SER   B 1 205 ? 28.043 -14.042 1.665   1.00 41.11  ? 898  SER   B OG  1 
ATOM   3840 N  N   . ASP   B 1 206 ? 29.445 -15.777 3.881   1.00 35.39  ? 899  ASP   B N   1 
ATOM   3841 C  CA  . ASP   B 1 206 ? 30.232 -15.572 5.081   1.00 35.26  ? 899  ASP   B CA  1 
ATOM   3842 C  C   . ASP   B 1 206 ? 31.032 -16.836 5.402   1.00 35.95  ? 899  ASP   B C   1 
ATOM   3843 O  O   . ASP   B 1 206 ? 32.157 -16.724 5.872   1.00 35.67  ? 899  ASP   B O   1 
ATOM   3844 C  CB  . ASP   B 1 206 ? 29.314 -15.221 6.256   1.00 35.86  ? 899  ASP   B CB  1 
ATOM   3845 C  CG  . ASP   B 1 206 ? 28.944 -13.760 6.380   1.00 37.56  ? 899  ASP   B CG  1 
ATOM   3846 O  OD1 . ASP   B 1 206 ? 29.489 -12.941 5.608   1.00 37.29  ? 899  ASP   B OD1 1 
ATOM   3847 O  OD2 . ASP   B 1 206 ? 28.118 -13.431 7.264   1.00 38.35  ? 899  ASP   B OD2 1 
ATOM   3848 N  N   . VAL   B 1 207 ? 30.462 -18.040 5.136   1.00 36.49  ? 900  VAL   B N   1 
ATOM   3849 C  CA  . VAL   B 1 207 ? 31.149 -19.317 5.321   1.00 36.65  ? 900  VAL   B CA  1 
ATOM   3850 C  C   . VAL   B 1 207 ? 32.358 -19.361 4.382   1.00 36.90  ? 900  VAL   B C   1 
ATOM   3851 O  O   . VAL   B 1 207 ? 33.443 -19.753 4.816   1.00 37.28  ? 900  VAL   B O   1 
ATOM   3852 C  CB  . VAL   B 1 207 ? 30.227 -20.529 5.097   1.00 37.25  ? 900  VAL   B CB  1 
ATOM   3853 C  CG1 . VAL   B 1 207 ? 30.987 -21.828 5.326   1.00 37.98  ? 900  VAL   B CG1 1 
ATOM   3854 C  CG2 . VAL   B 1 207 ? 29.011 -20.466 6.002   1.00 37.77  ? 900  VAL   B CG2 1 
ATOM   3855 N  N   . TRP   B 1 208 ? 32.217 -18.865 3.123   1.00 36.43  ? 901  TRP   B N   1 
ATOM   3856 C  CA  . TRP   B 1 208 ? 33.342 -18.805 2.179   1.00 37.02  ? 901  TRP   B CA  1 
ATOM   3857 C  C   . TRP   B 1 208 ? 34.516 -18.034 2.783   1.00 38.71  ? 901  TRP   B C   1 
ATOM   3858 O  O   . TRP   B 1 208 ? 35.627 -18.565 2.846   1.00 39.02  ? 901  TRP   B O   1 
ATOM   3859 C  CB  . TRP   B 1 208 ? 32.944 -18.170 0.835   1.00 36.38  ? 901  TRP   B CB  1 
ATOM   3860 C  CG  . TRP   B 1 208 ? 34.066 -18.202 -0.168  1.00 36.28  ? 901  TRP   B CG  1 
ATOM   3861 C  CD1 . TRP   B 1 208 ? 35.300 -17.629 -0.042  1.00 37.04  ? 901  TRP   B CD1 1 
ATOM   3862 C  CD2 . TRP   B 1 208 ? 34.078 -18.905 -1.416  1.00 35.82  ? 901  TRP   B CD2 1 
ATOM   3863 N  NE1 . TRP   B 1 208 ? 36.081 -17.943 -1.129  1.00 37.07  ? 901  TRP   B NE1 1 
ATOM   3864 C  CE2 . TRP   B 1 208 ? 35.348 -18.708 -1.997  1.00 36.37  ? 901  TRP   B CE2 1 
ATOM   3865 C  CE3 . TRP   B 1 208 ? 33.120 -19.637 -2.127  1.00 36.09  ? 901  TRP   B CE3 1 
ATOM   3866 C  CZ2 . TRP   B 1 208 ? 35.694 -19.254 -3.230  1.00 36.42  ? 901  TRP   B CZ2 1 
ATOM   3867 C  CZ3 . TRP   B 1 208 ? 33.465 -20.164 -3.352  1.00 36.51  ? 901  TRP   B CZ3 1 
ATOM   3868 C  CH2 . TRP   B 1 208 ? 34.732 -19.957 -3.897  1.00 36.44  ? 901  TRP   B CH2 1 
ATOM   3869 N  N   . SER   B 1 209 ? 34.236 -16.811 3.297   1.00 39.13  ? 902  SER   B N   1 
ATOM   3870 C  CA  . SER   B 1 209 ? 35.201 -15.933 3.952   1.00 39.17  ? 902  SER   B CA  1 
ATOM   3871 C  C   . SER   B 1 209 ? 35.767 -16.571 5.213   1.00 39.26  ? 902  SER   B C   1 
ATOM   3872 O  O   . SER   B 1 209 ? 36.939 -16.380 5.508   1.00 39.56  ? 902  SER   B O   1 
ATOM   3873 C  CB  . SER   B 1 209 ? 34.543 -14.607 4.289   1.00 40.75  ? 902  SER   B CB  1 
ATOM   3874 O  OG  . SER   B 1 209 ? 33.903 -14.073 3.141   1.00 43.99  ? 902  SER   B OG  1 
ATOM   3875 N  N   . TYR   B 1 210 ? 34.951 -17.363 5.932   1.00 38.84  ? 903  TYR   B N   1 
ATOM   3876 C  CA  . TYR   B 1 210 ? 35.370 -18.110 7.114   1.00 38.56  ? 903  TYR   B CA  1 
ATOM   3877 C  C   . TYR   B 1 210 ? 36.431 -19.135 6.725   1.00 39.00  ? 903  TYR   B C   1 
ATOM   3878 O  O   . TYR   B 1 210 ? 37.411 -19.277 7.438   1.00 39.14  ? 903  TYR   B O   1 
ATOM   3879 C  CB  . TYR   B 1 210 ? 34.169 -18.780 7.815   1.00 37.74  ? 903  TYR   B CB  1 
ATOM   3880 C  CG  . TYR   B 1 210 ? 34.570 -19.714 8.933   1.00 37.81  ? 903  TYR   B CG  1 
ATOM   3881 C  CD1 . TYR   B 1 210 ? 34.824 -19.235 10.211  1.00 38.26  ? 903  TYR   B CD1 1 
ATOM   3882 C  CD2 . TYR   B 1 210 ? 34.711 -21.077 8.710   1.00 38.32  ? 903  TYR   B CD2 1 
ATOM   3883 C  CE1 . TYR   B 1 210 ? 35.219 -20.086 11.236  1.00 38.60  ? 903  TYR   B CE1 1 
ATOM   3884 C  CE2 . TYR   B 1 210 ? 35.099 -21.938 9.728   1.00 38.82  ? 903  TYR   B CE2 1 
ATOM   3885 C  CZ  . TYR   B 1 210 ? 35.339 -21.440 10.994  1.00 39.16  ? 903  TYR   B CZ  1 
ATOM   3886 O  OH  . TYR   B 1 210 ? 35.725 -22.290 11.996  1.00 39.65  ? 903  TYR   B OH  1 
ATOM   3887 N  N   . GLY   B 1 211 ? 36.249 -19.812 5.594   1.00 39.14  ? 904  GLY   B N   1 
ATOM   3888 C  CA  . GLY   B 1 211 ? 37.227 -20.780 5.109   1.00 39.61  ? 904  GLY   B CA  1 
ATOM   3889 C  C   . GLY   B 1 211 ? 38.550 -20.114 4.779   1.00 39.95  ? 904  GLY   B C   1 
ATOM   3890 O  O   . GLY   B 1 211 ? 39.620 -20.649 5.075   1.00 40.39  ? 904  GLY   B O   1 
ATOM   3891 N  N   . VAL   B 1 212 ? 38.484 -18.908 4.203   1.00 39.42  ? 905  VAL   B N   1 
ATOM   3892 C  CA  . VAL   B 1 212 ? 39.681 -18.151 3.880   1.00 39.20  ? 905  VAL   B CA  1 
ATOM   3893 C  C   . VAL   B 1 212 ? 40.383 -17.733 5.171   1.00 38.88  ? 905  VAL   B C   1 
ATOM   3894 O  O   . VAL   B 1 212 ? 41.597 -17.876 5.271   1.00 39.06  ? 905  VAL   B O   1 
ATOM   3895 C  CB  . VAL   B 1 212 ? 39.370 -16.937 2.972   1.00 39.87  ? 905  VAL   B CB  1 
ATOM   3896 C  CG1 . VAL   B 1 212 ? 40.656 -16.269 2.513   1.00 40.41  ? 905  VAL   B CG1 1 
ATOM   3897 C  CG2 . VAL   B 1 212 ? 38.523 -17.344 1.771   1.00 40.32  ? 905  VAL   B CG2 1 
ATOM   3898 N  N   . THR   B 1 213 ? 39.605 -17.275 6.175   1.00 38.40  ? 906  THR   B N   1 
ATOM   3899 C  CA  . THR   B 1 213 ? 40.073 -16.845 7.491   1.00 38.56  ? 906  THR   B CA  1 
ATOM   3900 C  C   . THR   B 1 213 ? 40.796 -17.987 8.185   1.00 39.49  ? 906  THR   B C   1 
ATOM   3901 O  O   . THR   B 1 213 ? 41.866 -17.788 8.754   1.00 39.71  ? 906  THR   B O   1 
ATOM   3902 C  CB  . THR   B 1 213 ? 38.883 -16.351 8.319   1.00 39.26  ? 906  THR   B CB  1 
ATOM   3903 O  OG1 . THR   B 1 213 ? 38.260 -15.248 7.650   1.00 40.42  ? 906  THR   B OG1 1 
ATOM   3904 C  CG2 . THR   B 1 213 ? 39.276 -15.950 9.725   1.00 39.02  ? 906  THR   B CG2 1 
ATOM   3905 N  N   . VAL   B 1 214 ? 40.239 -19.196 8.098   1.00 39.84  ? 907  VAL   B N   1 
ATOM   3906 C  CA  . VAL   B 1 214 ? 40.835 -20.391 8.676   1.00 40.44  ? 907  VAL   B CA  1 
ATOM   3907 C  C   . VAL   B 1 214 ? 42.161 -20.684 7.995   1.00 41.20  ? 907  VAL   B C   1 
ATOM   3908 O  O   . VAL   B 1 214 ? 43.153 -20.896 8.678   1.00 40.91  ? 907  VAL   B O   1 
ATOM   3909 C  CB  . VAL   B 1 214 ? 39.838 -21.571 8.626   1.00 41.05  ? 907  VAL   B CB  1 
ATOM   3910 C  CG1 . VAL   B 1 214 ? 40.535 -22.913 8.827   1.00 41.74  ? 907  VAL   B CG1 1 
ATOM   3911 C  CG2 . VAL   B 1 214 ? 38.730 -21.370 9.652   1.00 41.27  ? 907  VAL   B CG2 1 
ATOM   3912 N  N   . TRP   B 1 215 ? 42.201 -20.598 6.660   1.00 42.45  ? 908  TRP   B N   1 
ATOM   3913 C  CA  . TRP   B 1 215 ? 43.422 -20.791 5.872   1.00 43.83  ? 908  TRP   B CA  1 
ATOM   3914 C  C   . TRP   B 1 215 ? 44.507 -19.773 6.283   1.00 44.34  ? 908  TRP   B C   1 
ATOM   3915 O  O   . TRP   B 1 215 ? 45.667 -20.147 6.439   1.00 44.86  ? 908  TRP   B O   1 
ATOM   3916 C  CB  . TRP   B 1 215 ? 43.119 -20.692 4.367   1.00 44.36  ? 908  TRP   B CB  1 
ATOM   3917 C  CG  . TRP   B 1 215 ? 44.301 -20.971 3.486   1.00 45.66  ? 908  TRP   B CG  1 
ATOM   3918 C  CD1 . TRP   B 1 215 ? 44.681 -22.180 2.978   1.00 46.80  ? 908  TRP   B CD1 1 
ATOM   3919 C  CD2 . TRP   B 1 215 ? 45.242 -20.010 2.986   1.00 46.04  ? 908  TRP   B CD2 1 
ATOM   3920 N  NE1 . TRP   B 1 215 ? 45.815 -22.035 2.206   1.00 47.20  ? 908  TRP   B NE1 1 
ATOM   3921 C  CE2 . TRP   B 1 215 ? 46.184 -20.712 2.200   1.00 46.99  ? 908  TRP   B CE2 1 
ATOM   3922 C  CE3 . TRP   B 1 215 ? 45.386 -18.623 3.134   1.00 46.65  ? 908  TRP   B CE3 1 
ATOM   3923 C  CZ2 . TRP   B 1 215 ? 47.236 -20.066 1.543   1.00 47.50  ? 908  TRP   B CZ2 1 
ATOM   3924 C  CZ3 . TRP   B 1 215 ? 46.445 -17.991 2.506   1.00 47.60  ? 908  TRP   B CZ3 1 
ATOM   3925 C  CH2 . TRP   B 1 215 ? 47.343 -18.706 1.705   1.00 47.56  ? 908  TRP   B CH2 1 
ATOM   3926 N  N   . GLU   B 1 216 ? 44.133 -18.502 6.509   1.00 43.86  ? 909  GLU   B N   1 
ATOM   3927 C  CA  . GLU   B 1 216 ? 45.076 -17.481 6.967   1.00 43.94  ? 909  GLU   B CA  1 
ATOM   3928 C  C   . GLU   B 1 216 ? 45.714 -17.896 8.303   1.00 44.58  ? 909  GLU   B C   1 
ATOM   3929 O  O   . GLU   B 1 216 ? 46.897 -17.673 8.508   1.00 44.95  ? 909  GLU   B O   1 
ATOM   3930 C  CB  . GLU   B 1 216 ? 44.365 -16.139 7.175   1.00 45.35  ? 909  GLU   B CB  1 
ATOM   3931 C  CG  . GLU   B 1 216 ? 43.890 -15.436 5.920   1.00 48.86  ? 909  GLU   B CG  1 
ATOM   3932 C  CD  . GLU   B 1 216 ? 43.318 -14.060 6.211   1.00 53.75  ? 909  GLU   B CD  1 
ATOM   3933 O  OE1 . GLU   B 1 216 ? 42.079 -13.944 6.351   1.00 54.09  ? 909  GLU   B OE1 1 
ATOM   3934 O  OE2 . GLU   B 1 216 ? 44.112 -13.098 6.316   1.00 55.79  ? 909  GLU   B OE2 1 
ATOM   3935 N  N   . LEU   B 1 217 ? 44.929 -18.509 9.205   1.00 44.37  ? 910  LEU   B N   1 
ATOM   3936 C  CA  . LEU   B 1 217 ? 45.431 -18.954 10.498  1.00 44.46  ? 910  LEU   B CA  1 
ATOM   3937 C  C   . LEU   B 1 217 ? 46.361 -20.152 10.343  1.00 45.45  ? 910  LEU   B C   1 
ATOM   3938 O  O   . LEU   B 1 217 ? 47.447 -20.166 10.925  1.00 45.30  ? 910  LEU   B O   1 
ATOM   3939 C  CB  . LEU   B 1 217 ? 44.272 -19.308 11.450  1.00 43.86  ? 910  LEU   B CB  1 
ATOM   3940 C  CG  . LEU   B 1 217 ? 43.211 -18.251 11.687  1.00 44.00  ? 910  LEU   B CG  1 
ATOM   3941 C  CD1 . LEU   B 1 217 ? 42.195 -18.727 12.706  1.00 43.71  ? 910  LEU   B CD1 1 
ATOM   3942 C  CD2 . LEU   B 1 217 ? 43.832 -16.942 12.128  1.00 44.69  ? 910  LEU   B CD2 1 
ATOM   3943 N  N   . MET   B 1 218 ? 45.949 -21.152 9.546   1.00 46.25  ? 911  MET   B N   1 
ATOM   3944 C  CA  . MET   B 1 218 ? 46.743 -22.360 9.306   1.00 47.21  ? 911  MET   B CA  1 
ATOM   3945 C  C   . MET   B 1 218 ? 48.066 -22.086 8.596   1.00 48.47  ? 911  MET   B C   1 
ATOM   3946 O  O   . MET   B 1 218 ? 49.024 -22.844 8.769   1.00 48.56  ? 911  MET   B O   1 
ATOM   3947 C  CB  . MET   B 1 218 ? 45.923 -23.396 8.546   1.00 47.56  ? 911  MET   B CB  1 
ATOM   3948 C  CG  . MET   B 1 218 ? 44.640 -23.760 9.246   1.00 49.36  ? 911  MET   B CG  1 
ATOM   3949 S  SD  . MET   B 1 218 ? 44.907 -24.492 10.866  1.00 52.70  ? 911  MET   B SD  1 
ATOM   3950 C  CE  . MET   B 1 218 ? 43.225 -24.530 11.488  1.00 52.05  ? 911  MET   B CE  1 
ATOM   3951 N  N   . THR   B 1 219 ? 48.121 -21.002 7.800   1.00 48.91  ? 912  THR   B N   1 
ATOM   3952 C  CA  . THR   B 1 219 ? 49.344 -20.602 7.122   1.00 49.61  ? 912  THR   B CA  1 
ATOM   3953 C  C   . THR   B 1 219 ? 50.159 -19.567 7.937   1.00 50.96  ? 912  THR   B C   1 
ATOM   3954 O  O   . THR   B 1 219 ? 51.162 -19.069 7.426   1.00 51.77  ? 912  THR   B O   1 
ATOM   3955 C  CB  . THR   B 1 219 ? 49.016 -20.069 5.718   1.00 50.23  ? 912  THR   B CB  1 
ATOM   3956 O  OG1 . THR   B 1 219 ? 48.115 -18.969 5.830   1.00 50.97  ? 912  THR   B OG1 1 
ATOM   3957 C  CG2 . THR   B 1 219 ? 48.440 -21.138 4.802   1.00 50.22  ? 912  THR   B CG2 1 
ATOM   3958 N  N   . PHE   B 1 220 ? 49.727 -19.234 9.175   1.00 51.02  ? 913  PHE   B N   1 
ATOM   3959 C  CA  . PHE   B 1 220 ? 50.348 -18.262 10.074  1.00 51.84  ? 913  PHE   B CA  1 
ATOM   3960 C  C   . PHE   B 1 220 ? 50.439 -16.853 9.479   1.00 53.34  ? 913  PHE   B C   1 
ATOM   3961 O  O   . PHE   B 1 220 ? 51.466 -16.175 9.612   1.00 53.80  ? 913  PHE   B O   1 
ATOM   3962 C  CB  . PHE   B 1 220 ? 51.706 -18.737 10.594  1.00 51.29  ? 913  PHE   B CB  1 
ATOM   3963 C  CG  . PHE   B 1 220 ? 51.623 -20.028 11.364  1.00 51.39  ? 913  PHE   B CG  1 
ATOM   3964 C  CD1 . PHE   B 1 220 ? 51.175 -20.045 12.675  1.00 52.06  ? 913  PHE   B CD1 1 
ATOM   3965 C  CD2 . PHE   B 1 220 ? 52.006 -21.224 10.785  1.00 51.47  ? 913  PHE   B CD2 1 
ATOM   3966 C  CE1 . PHE   B 1 220 ? 51.116 -21.235 13.386  1.00 52.36  ? 913  PHE   B CE1 1 
ATOM   3967 C  CE2 . PHE   B 1 220 ? 51.935 -22.408 11.491  1.00 51.87  ? 913  PHE   B CE2 1 
ATOM   3968 C  CZ  . PHE   B 1 220 ? 51.493 -22.407 12.785  1.00 51.87  ? 913  PHE   B CZ  1 
ATOM   3969 N  N   . GLY   B 1 221 ? 49.355 -16.433 8.843   1.00 53.68  ? 914  GLY   B N   1 
ATOM   3970 C  CA  . GLY   B 1 221 ? 49.214 -15.094 8.299   1.00 54.77  ? 914  GLY   B CA  1 
ATOM   3971 C  C   . GLY   B 1 221 ? 49.621 -14.886 6.863   1.00 56.17  ? 914  GLY   B C   1 
ATOM   3972 O  O   . GLY   B 1 221 ? 50.020 -13.776 6.508   1.00 56.96  ? 914  GLY   B O   1 
ATOM   3973 N  N   . SER   B 1 222 ? 49.498 -15.916 6.012   1.00 56.32  ? 915  SER   B N   1 
ATOM   3974 C  CA  . SER   B 1 222 ? 49.856 -15.761 4.603   1.00 56.76  ? 915  SER   B CA  1 
ATOM   3975 C  C   . SER   B 1 222 ? 48.784 -15.007 3.816   1.00 57.07  ? 915  SER   B C   1 
ATOM   3976 O  O   . SER   B 1 222 ? 47.616 -15.018 4.191   1.00 57.23  ? 915  SER   B O   1 
ATOM   3977 C  CB  . SER   B 1 222 ? 50.168 -17.111 3.972   1.00 58.24  ? 915  SER   B CB  1 
ATOM   3978 O  OG  . SER   B 1 222 ? 51.340 -17.663 4.552   1.00 60.69  ? 915  SER   B OG  1 
ATOM   3979 N  N   . LYS   B 1 223 ? 49.187 -14.307 2.754   1.00 57.05  ? 916  LYS   B N   1 
ATOM   3980 C  CA  . LYS   B 1 223 ? 48.251 -13.555 1.926   1.00 57.51  ? 916  LYS   B CA  1 
ATOM   3981 C  C   . LYS   B 1 223 ? 47.592 -14.511 0.948   1.00 58.06  ? 916  LYS   B C   1 
ATOM   3982 O  O   . LYS   B 1 223 ? 48.297 -15.221 0.226   1.00 58.15  ? 916  LYS   B O   1 
ATOM   3983 C  CB  . LYS   B 1 223 ? 48.984 -12.438 1.167   1.00 59.19  ? 916  LYS   B CB  1 
ATOM   3984 C  CG  . LYS   B 1 223 ? 49.175 -11.169 1.986   1.00 63.01  ? 916  LYS   B CG  1 
ATOM   3985 C  CD  . LYS   B 1 223 ? 50.335 -10.331 1.477   1.00 67.80  ? 916  LYS   B CD  1 
ATOM   3986 C  CE  . LYS   B 1 223 ? 51.566 -10.465 2.351   1.00 72.47  ? 916  LYS   B CE  1 
ATOM   3987 N  NZ  . LYS   B 1 223 ? 52.136 -11.848 2.360   1.00 75.32  ? 916  LYS   B NZ  1 
ATOM   3988 N  N   . PRO   B 1 224 ? 46.246 -14.586 0.927   1.00 58.14  ? 917  PRO   B N   1 
ATOM   3989 C  CA  . PRO   B 1 224 ? 45.584 -15.516 -0.004  1.00 58.36  ? 917  PRO   B CA  1 
ATOM   3990 C  C   . PRO   B 1 224 ? 45.762 -15.078 -1.444  1.00 58.36  ? 917  PRO   B C   1 
ATOM   3991 O  O   . PRO   B 1 224 ? 45.682 -13.884 -1.711  1.00 58.56  ? 917  PRO   B O   1 
ATOM   3992 C  CB  . PRO   B 1 224 ? 44.113 -15.479 0.428   1.00 58.83  ? 917  PRO   B CB  1 
ATOM   3993 C  CG  . PRO   B 1 224 ? 43.949 -14.191 1.073   1.00 59.05  ? 917  PRO   B CG  1 
ATOM   3994 C  CD  . PRO   B 1 224 ? 45.264 -13.832 1.722   1.00 57.45  ? 917  PRO   B CD  1 
ATOM   3995 N  N   . TYR   B 1 225 ? 46.064 -16.031 -2.354  1.00 58.07  ? 918  TYR   B N   1 
ATOM   3996 C  CA  . TYR   B 1 225 ? 46.286 -15.786 -3.786  1.00 58.49  ? 918  TYR   B CA  1 
ATOM   3997 C  C   . TYR   B 1 225 ? 47.357 -14.715 -3.965  1.00 58.98  ? 918  TYR   B C   1 
ATOM   3998 O  O   . TYR   B 1 225 ? 47.144 -13.720 -4.657  1.00 58.92  ? 918  TYR   B O   1 
ATOM   3999 C  CB  . TYR   B 1 225 ? 44.979 -15.402 -4.519  1.00 58.23  ? 918  TYR   B CB  1 
ATOM   4000 C  CG  . TYR   B 1 225 ? 43.768 -16.219 -4.113  1.00 58.33  ? 918  TYR   B CG  1 
ATOM   4001 C  CD1 . TYR   B 1 225 ? 43.558 -17.492 -4.627  1.00 58.70  ? 918  TYR   B CD1 1 
ATOM   4002 C  CD2 . TYR   B 1 225 ? 42.819 -15.705 -3.239  1.00 58.78  ? 918  TYR   B CD2 1 
ATOM   4003 C  CE1 . TYR   B 1 225 ? 42.447 -18.243 -4.262  1.00 59.29  ? 918  TYR   B CE1 1 
ATOM   4004 C  CE2 . TYR   B 1 225 ? 41.708 -16.449 -2.863  1.00 59.47  ? 918  TYR   B CE2 1 
ATOM   4005 C  CZ  . TYR   B 1 225 ? 41.526 -17.718 -3.377  1.00 60.16  ? 918  TYR   B CZ  1 
ATOM   4006 O  OH  . TYR   B 1 225 ? 40.422 -18.442 -3.021  1.00 61.57  ? 918  TYR   B OH  1 
ATOM   4007 N  N   . ASP   B 1 226 ? 48.469 -14.884 -3.249  1.00 59.36  ? 919  ASP   B N   1 
ATOM   4008 C  CA  . ASP   B 1 226 ? 49.546 -13.907 -3.270  1.00 60.48  ? 919  ASP   B CA  1 
ATOM   4009 C  C   . ASP   B 1 226 ? 50.142 -13.752 -4.642  1.00 61.13  ? 919  ASP   B C   1 
ATOM   4010 O  O   . ASP   B 1 226 ? 50.591 -14.740 -5.231  1.00 61.56  ? 919  ASP   B O   1 
ATOM   4011 C  CB  . ASP   B 1 226 ? 50.640 -14.266 -2.254  1.00 62.54  ? 919  ASP   B CB  1 
ATOM   4012 C  CG  . ASP   B 1 226 ? 51.579 -13.116 -1.950  1.00 66.97  ? 919  ASP   B CG  1 
ATOM   4013 O  OD1 . ASP   B 1 226 ? 51.144 -11.953 -2.054  1.00 67.93  ? 919  ASP   B OD1 1 
ATOM   4014 O  OD2 . ASP   B 1 226 ? 52.741 -13.381 -1.596  1.00 69.09  ? 919  ASP   B OD2 1 
ATOM   4015 N  N   . GLY   B 1 227 ? 50.109 -12.520 -5.150  1.00 60.93  ? 920  GLY   B N   1 
ATOM   4016 C  CA  . GLY   B 1 227 ? 50.656 -12.202 -6.460  1.00 61.05  ? 920  GLY   B CA  1 
ATOM   4017 C  C   . GLY   B 1 227 ? 49.626 -12.173 -7.566  1.00 60.90  ? 920  GLY   B C   1 
ATOM   4018 O  O   . GLY   B 1 227 ? 49.824 -11.480 -8.562  1.00 61.54  ? 920  GLY   B O   1 
ATOM   4019 N  N   . ILE   B 1 228 ? 48.540 -12.948 -7.427  1.00 59.92  ? 921  ILE   B N   1 
ATOM   4020 C  CA  . ILE   B 1 228 ? 47.476 -12.994 -8.424  1.00 59.41  ? 921  ILE   B CA  1 
ATOM   4021 C  C   . ILE   B 1 228 ? 46.641 -11.727 -8.309  1.00 59.58  ? 921  ILE   B C   1 
ATOM   4022 O  O   . ILE   B 1 228 ? 46.259 -11.351 -7.210  1.00 59.78  ? 921  ILE   B O   1 
ATOM   4023 C  CB  . ILE   B 1 228 ? 46.609 -14.256 -8.218  1.00 59.32  ? 921  ILE   B CB  1 
ATOM   4024 C  CG1 . ILE   B 1 228 ? 47.469 -15.517 -8.273  1.00 60.00  ? 921  ILE   B CG1 1 
ATOM   4025 C  CG2 . ILE   B 1 228 ? 45.448 -14.309 -9.208  1.00 59.70  ? 921  ILE   B CG2 1 
ATOM   4026 C  CD1 . ILE   B 1 228 ? 46.730 -16.814 -7.955  1.00 61.30  ? 921  ILE   B CD1 1 
ATOM   4027 N  N   . PRO   B 1 229 ? 46.387 -11.024 -9.419  1.00 59.60  ? 922  PRO   B N   1 
ATOM   4028 C  CA  . PRO   B 1 229 ? 45.589 -9.790  -9.337  1.00 59.46  ? 922  PRO   B CA  1 
ATOM   4029 C  C   . PRO   B 1 229 ? 44.139 -10.082 -9.004  1.00 59.13  ? 922  PRO   B C   1 
ATOM   4030 O  O   . PRO   B 1 229 ? 43.594 -11.082 -9.464  1.00 59.03  ? 922  PRO   B O   1 
ATOM   4031 C  CB  . PRO   B 1 229 ? 45.717 -9.175  -10.740 1.00 60.38  ? 922  PRO   B CB  1 
ATOM   4032 C  CG  . PRO   B 1 229 ? 46.799 -9.958  -11.430 1.00 60.95  ? 922  PRO   B CG  1 
ATOM   4033 C  CD  . PRO   B 1 229 ? 46.812 -11.311 -10.800 1.00 59.36  ? 922  PRO   B CD  1 
ATOM   4034 N  N   . ALA   B 1 230 ? 43.510 -9.198  -8.236  1.00 59.05  ? 923  ALA   B N   1 
ATOM   4035 C  CA  . ALA   B 1 230 ? 42.113 -9.357  -7.846  1.00 59.80  ? 923  ALA   B CA  1 
ATOM   4036 C  C   . ALA   B 1 230 ? 41.176 -9.479  -9.050  1.00 60.02  ? 923  ALA   B C   1 
ATOM   4037 O  O   . ALA   B 1 230 ? 40.191 -10.216 -8.998  1.00 59.95  ? 923  ALA   B O   1 
ATOM   4038 C  CB  . ALA   B 1 230 ? 41.685 -8.199  -6.958  1.00 60.13  ? 923  ALA   B CB  1 
ATOM   4039 N  N   . SER   B 1 231 ? 41.506 -8.796  -10.142 1.00 60.21  ? 924  SER   B N   1 
ATOM   4040 C  CA  . SER   B 1 231 ? 40.722 -8.842  -11.371 1.00 61.11  ? 924  SER   B CA  1 
ATOM   4041 C  C   . SER   B 1 231 ? 40.628 -10.262 -11.968 1.00 61.63  ? 924  SER   B C   1 
ATOM   4042 O  O   . SER   B 1 231 ? 39.698 -10.540 -12.726 1.00 62.08  ? 924  SER   B O   1 
ATOM   4043 C  CB  . SER   B 1 231 ? 41.327 -7.900  -12.403 1.00 62.48  ? 924  SER   B CB  1 
ATOM   4044 O  OG  . SER   B 1 231 ? 42.675 -8.262  -12.661 1.00 64.96  ? 924  SER   B OG  1 
ATOM   4045 N  N   . GLU   B 1 232 ? 41.569 -11.157 -11.612 1.00 61.34  ? 925  GLU   B N   1 
ATOM   4046 C  CA  . GLU   B 1 232 ? 41.608 -12.524 -12.131 1.00 61.65  ? 925  GLU   B CA  1 
ATOM   4047 C  C   . GLU   B 1 232 ? 41.027 -13.584 -11.195 1.00 61.00  ? 925  GLU   B C   1 
ATOM   4048 O  O   . GLU   B 1 232 ? 40.943 -14.740 -11.601 1.00 61.13  ? 925  GLU   B O   1 
ATOM   4049 C  CB  . GLU   B 1 232 ? 43.063 -12.914 -12.438 1.00 64.61  ? 925  GLU   B CB  1 
ATOM   4050 C  CG  . GLU   B 1 232 ? 43.789 -11.937 -13.346 1.00 70.13  ? 925  GLU   B CG  1 
ATOM   4051 C  CD  . GLU   B 1 232 ? 45.216 -12.322 -13.679 1.00 76.95  ? 925  GLU   B CD  1 
ATOM   4052 O  OE1 . GLU   B 1 232 ? 45.648 -13.432 -13.287 1.00 77.76  ? 925  GLU   B OE1 1 
ATOM   4053 O  OE2 . GLU   B 1 232 ? 45.910 -11.502 -14.324 1.00 79.73  ? 925  GLU   B OE2 1 
ATOM   4054 N  N   . ILE   B 1 233 ? 40.675 -13.224 -9.946  1.00 60.18  ? 926  ILE   B N   1 
ATOM   4055 C  CA  . ILE   B 1 233 ? 40.218 -14.201 -8.952  1.00 59.56  ? 926  ILE   B CA  1 
ATOM   4056 C  C   . ILE   B 1 233 ? 38.963 -14.968 -9.386  1.00 59.17  ? 926  ILE   B C   1 
ATOM   4057 O  O   . ILE   B 1 233 ? 39.015 -16.196 -9.388  1.00 59.19  ? 926  ILE   B O   1 
ATOM   4058 C  CB  . ILE   B 1 233 ? 40.077 -13.583 -7.541  1.00 59.66  ? 926  ILE   B CB  1 
ATOM   4059 C  CG1 . ILE   B 1 233 ? 41.456 -13.128 -7.007  1.00 60.19  ? 926  ILE   B CG1 1 
ATOM   4060 C  CG2 . ILE   B 1 233 ? 39.402 -14.536 -6.550  1.00 59.99  ? 926  ILE   B CG2 1 
ATOM   4061 C  CD1 . ILE   B 1 233 ? 42.475 -14.207 -6.886  1.00 61.08  ? 926  ILE   B CD1 1 
ATOM   4062 N  N   . SER   B 1 234 ? 37.889 -14.296 -9.834  1.00 58.83  ? 927  SER   B N   1 
ATOM   4063 C  CA  . SER   B 1 234 ? 36.673 -15.004 -10.265 1.00 59.22  ? 927  SER   B CA  1 
ATOM   4064 C  C   . SER   B 1 234 ? 36.933 -16.060 -11.332 1.00 59.56  ? 927  SER   B C   1 
ATOM   4065 O  O   . SER   B 1 234 ? 36.346 -17.137 -11.290 1.00 59.64  ? 927  SER   B O   1 
ATOM   4066 C  CB  . SER   B 1 234 ? 35.609 -14.027 -10.749 1.00 60.78  ? 927  SER   B CB  1 
ATOM   4067 O  OG  . SER   B 1 234 ? 35.975 -13.452 -11.990 1.00 63.99  ? 927  SER   B OG  1 
ATOM   4068 N  N   . SER   B 1 235 ? 37.848 -15.765 -12.258 1.00 59.79  ? 928  SER   B N   1 
ATOM   4069 C  CA  . SER   B 1 235 ? 38.232 -16.691 -13.319 1.00 60.27  ? 928  SER   B CA  1 
ATOM   4070 C  C   . SER   B 1 235 ? 39.027 -17.876 -12.763 1.00 59.98  ? 928  SER   B C   1 
ATOM   4071 O  O   . SER   B 1 235 ? 38.875 -18.994 -13.247 1.00 60.06  ? 928  SER   B O   1 
ATOM   4072 C  CB  . SER   B 1 235 ? 39.048 -15.968 -14.382 1.00 62.07  ? 928  SER   B CB  1 
ATOM   4073 O  OG  . SER   B 1 235 ? 39.328 -16.860 -15.446 1.00 65.41  ? 928  SER   B OG  1 
ATOM   4074 N  N   . ILE   B 1 236 ? 39.873 -17.628 -11.754 1.00 59.41  ? 929  ILE   B N   1 
ATOM   4075 C  CA  . ILE   B 1 236 ? 40.650 -18.663 -11.068 1.00 59.39  ? 929  ILE   B CA  1 
ATOM   4076 C  C   . ILE   B 1 236 ? 39.668 -19.618 -10.370 1.00 58.36  ? 929  ILE   B C   1 
ATOM   4077 O  O   . ILE   B 1 236 ? 39.806 -20.835 -10.491 1.00 58.53  ? 929  ILE   B O   1 
ATOM   4078 C  CB  . ILE   B 1 236 ? 41.706 -18.004 -10.099 1.00 60.19  ? 929  ILE   B CB  1 
ATOM   4079 C  CG1 . ILE   B 1 236 ? 43.128 -18.136 -10.650 1.00 61.49  ? 929  ILE   B CG1 1 
ATOM   4080 C  CG2 . ILE   B 1 236 ? 41.641 -18.467 -8.631  1.00 60.34  ? 929  ILE   B CG2 1 
ATOM   4081 C  CD1 . ILE   B 1 236 ? 43.673 -16.843 -11.148 1.00 63.08  ? 929  ILE   B CD1 1 
ATOM   4082 N  N   . LEU   B 1 237 ? 38.647 -19.052 -9.695  1.00 57.19  ? 930  LEU   B N   1 
ATOM   4083 C  CA  . LEU   B 1 237 ? 37.638 -19.815 -8.969  1.00 56.52  ? 930  LEU   B CA  1 
ATOM   4084 C  C   . LEU   B 1 237 ? 36.813 -20.669 -9.918  1.00 55.98  ? 930  LEU   B C   1 
ATOM   4085 O  O   . LEU   B 1 237 ? 36.508 -21.820 -9.594  1.00 56.13  ? 930  LEU   B O   1 
ATOM   4086 C  CB  . LEU   B 1 237 ? 36.721 -18.881 -8.166  1.00 56.23  ? 930  LEU   B CB  1 
ATOM   4087 C  CG  . LEU   B 1 237 ? 37.390 -17.972 -7.139  1.00 56.82  ? 930  LEU   B CG  1 
ATOM   4088 C  CD1 . LEU   B 1 237 ? 36.355 -17.080 -6.449  1.00 56.95  ? 930  LEU   B CD1 1 
ATOM   4089 C  CD2 . LEU   B 1 237 ? 38.213 -18.775 -6.131  1.00 57.05  ? 930  LEU   B CD2 1 
ATOM   4090 N  N   . GLU   B 1 238 ? 36.475 -20.119 -11.096 1.00 54.94  ? 931  GLU   B N   1 
ATOM   4091 C  CA  . GLU   B 1 238 ? 35.700 -20.834 -12.111 1.00 54.37  ? 931  GLU   B CA  1 
ATOM   4092 C  C   . GLU   B 1 238 ? 36.478 -22.011 -12.701 1.00 53.08  ? 931  GLU   B C   1 
ATOM   4093 O  O   . GLU   B 1 238 ? 35.894 -23.057 -12.975 1.00 52.68  ? 931  GLU   B O   1 
ATOM   4094 C  CB  . GLU   B 1 238 ? 35.216 -19.868 -13.198 1.00 56.63  ? 931  GLU   B CB  1 
ATOM   4095 C  CG  . GLU   B 1 238 ? 33.969 -19.130 -12.768 1.00 62.15  ? 931  GLU   B CG  1 
ATOM   4096 C  CD  . GLU   B 1 238 ? 33.722 -17.833 -13.501 1.00 71.65  ? 931  GLU   B CD  1 
ATOM   4097 O  OE1 . GLU   B 1 238 ? 32.551 -17.575 -13.864 1.00 73.84  ? 931  GLU   B OE1 1 
ATOM   4098 O  OE2 . GLU   B 1 238 ? 34.695 -17.072 -13.707 1.00 75.14  ? 931  GLU   B OE2 1 
ATOM   4099 N  N   . LYS   B 1 239 ? 37.805 -21.860 -12.841 1.00 52.30  ? 932  LYS   B N   1 
ATOM   4100 C  CA  . LYS   B 1 239 ? 38.669 -22.942 -13.327 1.00 51.85  ? 932  LYS   B CA  1 
ATOM   4101 C  C   . LYS   B 1 239 ? 38.845 -24.079 -12.316 1.00 51.04  ? 932  LYS   B C   1 
ATOM   4102 O  O   . LYS   B 1 239 ? 39.388 -25.121 -12.682 1.00 51.50  ? 932  LYS   B O   1 
ATOM   4103 C  CB  . LYS   B 1 239 ? 40.051 -22.410 -13.744 1.00 54.01  ? 932  LYS   B CB  1 
ATOM   4104 C  CG  . LYS   B 1 239 ? 40.046 -21.641 -15.062 1.00 58.92  ? 932  LYS   B CG  1 
ATOM   4105 C  CD  . LYS   B 1 239 ? 41.459 -21.335 -15.563 1.00 64.58  ? 932  LYS   B CD  1 
ATOM   4106 C  CE  . LYS   B 1 239 ? 42.210 -20.357 -14.680 1.00 69.09  ? 932  LYS   B CE  1 
ATOM   4107 N  NZ  . LYS   B 1 239 ? 43.496 -19.910 -15.296 1.00 71.08  ? 932  LYS   B NZ  1 
ATOM   4108 N  N   . GLY   B 1 240 ? 38.415 -23.873 -11.063 1.00 49.80  ? 933  GLY   B N   1 
ATOM   4109 C  CA  . GLY   B 1 240 ? 38.527 -24.857 -9.993  1.00 48.80  ? 933  GLY   B CA  1 
ATOM   4110 C  C   . GLY   B 1 240 ? 39.739 -24.679 -9.098  1.00 47.72  ? 933  GLY   B C   1 
ATOM   4111 O  O   . GLY   B 1 240 ? 40.060 -25.569 -8.305  1.00 47.61  ? 933  GLY   B O   1 
ATOM   4112 N  N   . GLU   B 1 241 ? 40.423 -23.533 -9.208  1.00 46.81  ? 934  GLU   B N   1 
ATOM   4113 C  CA  . GLU   B 1 241 ? 41.584 -23.257 -8.381  1.00 46.67  ? 934  GLU   B CA  1 
ATOM   4114 C  C   . GLU   B 1 241 ? 41.137 -22.766 -7.001  1.00 45.55  ? 934  GLU   B C   1 
ATOM   4115 O  O   . GLU   B 1 241 ? 40.234 -21.936 -6.882  1.00 45.34  ? 934  GLU   B O   1 
ATOM   4116 C  CB  . GLU   B 1 241 ? 42.492 -22.217 -9.047  1.00 49.94  ? 934  GLU   B CB  1 
ATOM   4117 C  CG  . GLU   B 1 241 ? 43.081 -22.678 -10.365 1.00 57.83  ? 934  GLU   B CG  1 
ATOM   4118 C  CD  . GLU   B 1 241 ? 44.168 -21.766 -10.903 1.00 67.94  ? 934  GLU   B CD  1 
ATOM   4119 O  OE1 . GLU   B 1 241 ? 45.010 -21.303 -10.097 1.00 69.37  ? 934  GLU   B OE1 1 
ATOM   4120 O  OE2 . GLU   B 1 241 ? 44.181 -21.520 -12.133 1.00 71.51  ? 934  GLU   B OE2 1 
ATOM   4121 N  N   . ARG   B 1 242 ? 41.749 -23.304 -5.961  1.00 44.46  ? 935  ARG   B N   1 
ATOM   4122 C  CA  . ARG   B 1 242 ? 41.451 -22.927 -4.583  1.00 43.80  ? 935  ARG   B CA  1 
ATOM   4123 C  C   . ARG   B 1 242 ? 42.757 -22.687 -3.819  1.00 44.81  ? 935  ARG   B C   1 
ATOM   4124 O  O   . ARG   B 1 242 ? 43.843 -23.050 -4.289  1.00 45.54  ? 935  ARG   B O   1 
ATOM   4125 C  CB  . ARG   B 1 242 ? 40.629 -24.026 -3.881  1.00 42.54  ? 935  ARG   B CB  1 
ATOM   4126 C  CG  . ARG   B 1 242 ? 39.247 -24.252 -4.454  1.00 42.16  ? 935  ARG   B CG  1 
ATOM   4127 C  CD  . ARG   B 1 242 ? 38.390 -23.015 -4.365  1.00 42.33  ? 935  ARG   B CD  1 
ATOM   4128 N  NE  . ARG   B 1 242 ? 37.017 -23.252 -4.806  1.00 41.57  ? 935  ARG   B NE  1 
ATOM   4129 C  CZ  . ARG   B 1 242 ? 36.607 -23.186 -6.067  1.00 40.76  ? 935  ARG   B CZ  1 
ATOM   4130 N  NH1 . ARG   B 1 242 ? 35.334 -23.392 -6.365  1.00 39.90  ? 935  ARG   B NH1 1 
ATOM   4131 N  NH2 . ARG   B 1 242 ? 37.469 -22.907 -7.040  1.00 39.00  ? 935  ARG   B NH2 1 
ATOM   4132 N  N   . LEU   B 1 243 ? 42.665 -22.101 -2.621  1.00 44.58  ? 936  LEU   B N   1 
ATOM   4133 C  CA  . LEU   B 1 243 ? 43.838 -21.865 -1.783  1.00 44.38  ? 936  LEU   B CA  1 
ATOM   4134 C  C   . LEU   B 1 243 ? 44.522 -23.198 -1.447  1.00 44.92  ? 936  LEU   B C   1 
ATOM   4135 O  O   . LEU   B 1 243 ? 43.844 -24.198 -1.203  1.00 44.69  ? 936  LEU   B O   1 
ATOM   4136 C  CB  . LEU   B 1 243 ? 43.423 -21.131 -0.502  1.00 43.52  ? 936  LEU   B CB  1 
ATOM   4137 C  CG  . LEU   B 1 243 ? 43.101 -19.660 -0.676  1.00 43.91  ? 936  LEU   B CG  1 
ATOM   4138 C  CD1 . LEU   B 1 243 ? 42.572 -19.071 0.606   1.00 44.20  ? 936  LEU   B CD1 1 
ATOM   4139 C  CD2 . LEU   B 1 243 ? 44.312 -18.897 -1.129  1.00 44.41  ? 936  LEU   B CD2 1 
ATOM   4140 N  N   . PRO   B 1 244 ? 45.856 -23.252 -1.547  1.00 45.11  ? 937  PRO   B N   1 
ATOM   4141 C  CA  . PRO   B 1 244 ? 46.557 -24.521 -1.278  1.00 45.30  ? 937  PRO   B CA  1 
ATOM   4142 C  C   . PRO   B 1 244 ? 46.377 -25.061 0.134   1.00 46.41  ? 937  PRO   B C   1 
ATOM   4143 O  O   . PRO   B 1 244 ? 46.028 -24.328 1.052   1.00 46.91  ? 937  PRO   B O   1 
ATOM   4144 C  CB  . PRO   B 1 244 ? 48.024 -24.191 -1.553  1.00 45.67  ? 937  PRO   B CB  1 
ATOM   4145 C  CG  . PRO   B 1 244 ? 48.111 -22.684 -1.426  1.00 46.25  ? 937  PRO   B CG  1 
ATOM   4146 C  CD  . PRO   B 1 244 ? 46.788 -22.158 -1.888  1.00 44.56  ? 937  PRO   B CD  1 
ATOM   4147 N  N   . GLN   B 1 245 ? 46.610 -26.353 0.300   1.00 46.78  ? 938  GLN   B N   1 
ATOM   4148 C  CA  . GLN   B 1 245 ? 46.514 -27.005 1.592   1.00 47.64  ? 938  GLN   B CA  1 
ATOM   4149 C  C   . GLN   B 1 245 ? 47.720 -26.616 2.442   1.00 49.01  ? 938  GLN   B C   1 
ATOM   4150 O  O   . GLN   B 1 245 ? 48.858 -26.813 2.012   1.00 49.28  ? 938  GLN   B O   1 
ATOM   4151 C  CB  . GLN   B 1 245 ? 46.457 -28.520 1.391   1.00 48.89  ? 938  GLN   B CB  1 
ATOM   4152 C  CG  . GLN   B 1 245 ? 46.492 -29.320 2.685   1.00 52.70  ? 938  GLN   B CG  1 
ATOM   4153 C  CD  . GLN   B 1 245 ? 46.451 -30.821 2.501   1.00 58.30  ? 938  GLN   B CD  1 
ATOM   4154 O  OE1 . GLN   B 1 245 ? 46.550 -31.572 3.476   1.00 61.38  ? 938  GLN   B OE1 1 
ATOM   4155 N  NE2 . GLN   B 1 245 ? 46.298 -31.309 1.267   1.00 58.64  ? 938  GLN   B NE2 1 
ATOM   4156 N  N   . PRO   B 1 246 ? 47.503 -26.019 3.632   1.00 49.68  ? 939  PRO   B N   1 
ATOM   4157 C  CA  . PRO   B 1 246 ? 48.649 -25.607 4.463   1.00 50.11  ? 939  PRO   B CA  1 
ATOM   4158 C  C   . PRO   B 1 246 ? 49.468 -26.802 4.941   1.00 51.02  ? 939  PRO   B C   1 
ATOM   4159 O  O   . PRO   B 1 246 ? 48.923 -27.878 5.186   1.00 51.14  ? 939  PRO   B O   1 
ATOM   4160 C  CB  . PRO   B 1 246 ? 47.998 -24.837 5.619   1.00 50.46  ? 939  PRO   B CB  1 
ATOM   4161 C  CG  . PRO   B 1 246 ? 46.623 -24.492 5.124   1.00 50.79  ? 939  PRO   B CG  1 
ATOM   4162 C  CD  . PRO   B 1 246 ? 46.225 -25.648 4.264   1.00 49.24  ? 939  PRO   B CD  1 
ATOM   4163 N  N   . PRO   B 1 247 ? 50.799 -26.647 5.014   1.00 51.39  ? 940  PRO   B N   1 
ATOM   4164 C  CA  . PRO   B 1 247 ? 51.651 -27.775 5.416   1.00 51.88  ? 940  PRO   B CA  1 
ATOM   4165 C  C   . PRO   B 1 247 ? 51.291 -28.452 6.741   1.00 52.41  ? 940  PRO   B C   1 
ATOM   4166 O  O   . PRO   B 1 247 ? 51.458 -29.666 6.846   1.00 52.94  ? 940  PRO   B O   1 
ATOM   4167 C  CB  . PRO   B 1 247 ? 53.050 -27.153 5.450   1.00 52.37  ? 940  PRO   B CB  1 
ATOM   4168 C  CG  . PRO   B 1 247 ? 52.971 -26.033 4.477   1.00 52.49  ? 940  PRO   B CG  1 
ATOM   4169 C  CD  . PRO   B 1 247 ? 51.606 -25.462 4.682   1.00 50.85  ? 940  PRO   B CD  1 
ATOM   4170 N  N   . ILE   B 1 248 ? 50.776 -27.703 7.738   1.00 52.08  ? 941  ILE   B N   1 
ATOM   4171 C  CA  . ILE   B 1 248 ? 50.399 -28.309 9.014   1.00 52.12  ? 941  ILE   B CA  1 
ATOM   4172 C  C   . ILE   B 1 248 ? 49.090 -29.092 8.963   1.00 52.26  ? 941  ILE   B C   1 
ATOM   4173 O  O   . ILE   B 1 248 ? 48.851 -29.926 9.833   1.00 52.84  ? 941  ILE   B O   1 
ATOM   4174 C  CB  . ILE   B 1 248 ? 50.363 -27.271 10.153  1.00 52.79  ? 941  ILE   B CB  1 
ATOM   4175 C  CG1 . ILE   B 1 248 ? 49.197 -26.285 9.983   1.00 53.72  ? 941  ILE   B CG1 1 
ATOM   4176 C  CG2 . ILE   B 1 248 ? 51.702 -26.563 10.290  1.00 53.58  ? 941  ILE   B CG2 1 
ATOM   4177 C  CD1 . ILE   B 1 248 ? 49.004 -25.347 11.144  1.00 55.14  ? 941  ILE   B CD1 1 
ATOM   4178 N  N   . CYS   B 1 249 ? 48.233 -28.825 7.975   1.00 51.83  ? 942  CYS   B N   1 
ATOM   4179 C  CA  . CYS   B 1 249 ? 46.919 -29.453 7.909   1.00 51.98  ? 942  CYS   B CA  1 
ATOM   4180 C  C   . CYS   B 1 249 ? 46.878 -30.865 7.406   1.00 52.39  ? 942  CYS   B C   1 
ATOM   4181 O  O   . CYS   B 1 249 ? 47.371 -31.170 6.318   1.00 53.00  ? 942  CYS   B O   1 
ATOM   4182 C  CB  . CYS   B 1 249 ? 45.964 -28.595 7.099   1.00 52.21  ? 942  CYS   B CB  1 
ATOM   4183 S  SG  . CYS   B 1 249 ? 45.760 -26.941 7.761   1.00 56.32  ? 942  CYS   B SG  1 
ATOM   4184 N  N   . THR   B 1 250 ? 46.139 -31.699 8.139   1.00 51.75  ? 943  THR   B N   1 
ATOM   4185 C  CA  . THR   B 1 250 ? 45.805 -33.033 7.680   1.00 51.32  ? 943  THR   B CA  1 
ATOM   4186 C  C   . THR   B 1 250 ? 44.677 -32.840 6.640   1.00 51.09  ? 943  THR   B C   1 
ATOM   4187 O  O   . THR   B 1 250 ? 44.107 -31.743 6.532   1.00 51.02  ? 943  THR   B O   1 
ATOM   4188 C  CB  . THR   B 1 250 ? 45.350 -33.899 8.856   1.00 52.14  ? 943  THR   B CB  1 
ATOM   4189 O  OG1 . THR   B 1 250 ? 44.258 -33.252 9.518   1.00 52.87  ? 943  THR   B OG1 1 
ATOM   4190 C  CG2 . THR   B 1 250 ? 46.477 -34.187 9.826   1.00 52.42  ? 943  THR   B CG2 1 
ATOM   4191 N  N   . ILE   B 1 251 ? 44.354 -33.886 5.874   1.00 51.18  ? 944  ILE   B N   1 
ATOM   4192 C  CA  . ILE   B 1 251 ? 43.315 -33.752 4.862   1.00 51.73  ? 944  ILE   B CA  1 
ATOM   4193 C  C   . ILE   B 1 251 ? 41.923 -33.523 5.510   1.00 51.61  ? 944  ILE   B C   1 
ATOM   4194 O  O   . ILE   B 1 251 ? 41.086 -32.867 4.890   1.00 51.70  ? 944  ILE   B O   1 
ATOM   4195 C  CB  . ILE   B 1 251 ? 43.354 -34.892 3.830   1.00 52.46  ? 944  ILE   B CB  1 
ATOM   4196 C  CG1 . ILE   B 1 251 ? 42.602 -34.512 2.559   1.00 53.94  ? 944  ILE   B CG1 1 
ATOM   4197 C  CG2 . ILE   B 1 251 ? 42.816 -36.132 4.409   1.00 52.77  ? 944  ILE   B CG2 1 
ATOM   4198 C  CD1 . ILE   B 1 251 ? 43.137 -33.295 1.849   1.00 55.60  ? 944  ILE   B CD1 1 
ATOM   4199 N  N   . ASP   B 1 252 ? 41.720 -33.955 6.780   1.00 50.81  ? 945  ASP   B N   1 
ATOM   4200 C  CA  . ASP   B 1 252 ? 40.461 -33.764 7.507   1.00 50.64  ? 945  ASP   B CA  1 
ATOM   4201 C  C   . ASP   B 1 252 ? 40.162 -32.282 7.707   1.00 49.94  ? 945  ASP   B C   1 
ATOM   4202 O  O   . ASP   B 1 252 ? 39.018 -31.857 7.547   1.00 50.28  ? 945  ASP   B O   1 
ATOM   4203 C  CB  . ASP   B 1 252 ? 40.526 -34.436 8.885   1.00 53.05  ? 945  ASP   B CB  1 
ATOM   4204 C  CG  . ASP   B 1 252 ? 40.874 -35.898 8.872   1.00 58.89  ? 945  ASP   B CG  1 
ATOM   4205 O  OD1 . ASP   B 1 252 ? 41.989 -36.246 8.383   1.00 59.72  ? 945  ASP   B OD1 1 
ATOM   4206 O  OD2 . ASP   B 1 252 ? 40.059 -36.701 9.388   1.00 61.40  ? 945  ASP   B OD2 1 
ATOM   4207 N  N   . VAL   B 1 253 ? 41.196 -31.503 8.074   1.00 48.77  ? 946  VAL   B N   1 
ATOM   4208 C  CA  . VAL   B 1 253 ? 41.103 -30.073 8.307   1.00 48.09  ? 946  VAL   B CA  1 
ATOM   4209 C  C   . VAL   B 1 253 ? 40.963 -29.341 6.982   1.00 47.23  ? 946  VAL   B C   1 
ATOM   4210 O  O   . VAL   B 1 253 ? 40.130 -28.447 6.865   1.00 47.10  ? 946  VAL   B O   1 
ATOM   4211 C  CB  . VAL   B 1 253 ? 42.326 -29.576 9.121   1.00 48.89  ? 946  VAL   B CB  1 
ATOM   4212 C  CG1 . VAL   B 1 253 ? 42.250 -28.075 9.393   1.00 49.15  ? 946  VAL   B CG1 1 
ATOM   4213 C  CG2 . VAL   B 1 253 ? 42.450 -30.352 10.424  1.00 49.29  ? 946  VAL   B CG2 1 
ATOM   4214 N  N   . TYR   B 1 254 ? 41.748 -29.741 5.971   1.00 46.78  ? 947  TYR   B N   1 
ATOM   4215 C  CA  . TYR   B 1 254 ? 41.686 -29.101 4.659   1.00 46.61  ? 947  TYR   B CA  1 
ATOM   4216 C  C   . TYR   B 1 254 ? 40.351 -29.304 3.946   1.00 45.17  ? 947  TYR   B C   1 
ATOM   4217 O  O   . TYR   B 1 254 ? 39.874 -28.393 3.279   1.00 45.31  ? 947  TYR   B O   1 
ATOM   4218 C  CB  . TYR   B 1 254 ? 42.858 -29.503 3.757   1.00 47.48  ? 947  TYR   B CB  1 
ATOM   4219 C  CG  . TYR   B 1 254 ? 42.841 -28.756 2.437   1.00 49.53  ? 947  TYR   B CG  1 
ATOM   4220 C  CD1 . TYR   B 1 254 ? 43.004 -27.376 2.394   1.00 51.34  ? 947  TYR   B CD1 1 
ATOM   4221 C  CD2 . TYR   B 1 254 ? 42.583 -29.417 1.242   1.00 50.44  ? 947  TYR   B CD2 1 
ATOM   4222 C  CE1 . TYR   B 1 254 ? 42.957 -26.678 1.190   1.00 52.43  ? 947  TYR   B CE1 1 
ATOM   4223 C  CE2 . TYR   B 1 254 ? 42.529 -28.728 0.034   1.00 51.69  ? 947  TYR   B CE2 1 
ATOM   4224 C  CZ  . TYR   B 1 254 ? 42.730 -27.360 0.010   1.00 53.33  ? 947  TYR   B CZ  1 
ATOM   4225 O  OH  . TYR   B 1 254 ? 42.684 -26.665 -1.181  1.00 55.62  ? 947  TYR   B OH  1 
ATOM   4226 N  N   . MET   B 1 255 ? 39.737 -30.464 4.103   1.00 44.14  ? 948  MET   B N   1 
ATOM   4227 C  CA  . MET   B 1 255 ? 38.445 -30.722 3.487   1.00 43.87  ? 948  MET   B CA  1 
ATOM   4228 C  C   . MET   B 1 255 ? 37.366 -29.786 4.017   1.00 43.52  ? 948  MET   B C   1 
ATOM   4229 O  O   . MET   B 1 255 ? 36.506 -29.395 3.242   1.00 43.79  ? 948  MET   B O   1 
ATOM   4230 C  CB  . MET   B 1 255 ? 38.065 -32.197 3.590   1.00 44.61  ? 948  MET   B CB  1 
ATOM   4231 C  CG  . MET   B 1 255 ? 38.865 -33.080 2.643   1.00 46.96  ? 948  MET   B CG  1 
ATOM   4232 S  SD  . MET   B 1 255 ? 38.521 -32.713 0.905   1.00 53.00  ? 948  MET   B SD  1 
ATOM   4233 C  CE  . MET   B 1 255 ? 40.045 -31.920 0.420   1.00 51.22  ? 948  MET   B CE  1 
ATOM   4234 N  N   . ILE   B 1 256 ? 37.452 -29.359 5.300   1.00 42.74  ? 949  ILE   B N   1 
ATOM   4235 C  CA  . ILE   B 1 256 ? 36.508 -28.392 5.877   1.00 42.27  ? 949  ILE   B CA  1 
ATOM   4236 C  C   . ILE   B 1 256 ? 36.648 -27.061 5.154   1.00 40.95  ? 949  ILE   B C   1 
ATOM   4237 O  O   . ILE   B 1 256 ? 35.647 -26.469 4.759   1.00 40.49  ? 949  ILE   B O   1 
ATOM   4238 C  CB  . ILE   B 1 256 ? 36.692 -28.199 7.408   1.00 43.12  ? 949  ILE   B CB  1 
ATOM   4239 C  CG1 . ILE   B 1 256 ? 36.484 -29.518 8.177   1.00 44.18  ? 949  ILE   B CG1 1 
ATOM   4240 C  CG2 . ILE   B 1 256 ? 35.750 -27.134 7.907   1.00 43.89  ? 949  ILE   B CG2 1 
ATOM   4241 C  CD1 . ILE   B 1 256 ? 36.597 -29.430 9.719   1.00 45.39  ? 949  ILE   B CD1 1 
ATOM   4242 N  N   . MET   B 1 257 ? 37.901 -26.616 4.954   1.00 40.49  ? 950  MET   B N   1 
ATOM   4243 C  CA  . MET   B 1 257 ? 38.221 -25.372 4.253   1.00 40.51  ? 950  MET   B CA  1 
ATOM   4244 C  C   . MET   B 1 257 ? 37.705 -25.433 2.836   1.00 40.03  ? 950  MET   B C   1 
ATOM   4245 O  O   . MET   B 1 257 ? 36.926 -24.574 2.439   1.00 40.57  ? 950  MET   B O   1 
ATOM   4246 C  CB  . MET   B 1 257 ? 39.735 -25.123 4.219   1.00 41.30  ? 950  MET   B CB  1 
ATOM   4247 C  CG  . MET   B 1 257 ? 40.333 -24.929 5.549   1.00 44.79  ? 950  MET   B CG  1 
ATOM   4248 S  SD  . MET   B 1 257 ? 42.006 -24.334 5.298   1.00 53.40  ? 950  MET   B SD  1 
ATOM   4249 C  CE  . MET   B 1 257 ? 42.868 -25.464 6.332   1.00 47.31  ? 950  MET   B CE  1 
ATOM   4250 N  N   . ARG   B 1 258 ? 38.090 -26.485 2.096   1.00 38.90  ? 951  ARG   B N   1 
ATOM   4251 C  CA  . ARG   B 1 258 ? 37.731 -26.750 0.712   1.00 38.12  ? 951  ARG   B CA  1 
ATOM   4252 C  C   . ARG   B 1 258 ? 36.219 -26.711 0.531   1.00 38.28  ? 951  ARG   B C   1 
ATOM   4253 O  O   . ARG   B 1 258 ? 35.741 -26.156 -0.452  1.00 38.43  ? 951  ARG   B O   1 
ATOM   4254 C  CB  . ARG   B 1 258 ? 38.351 -28.099 0.284   1.00 38.79  ? 951  ARG   B CB  1 
ATOM   4255 C  CG  . ARG   B 1 258 ? 38.186 -28.530 -1.178  1.00 40.86  ? 951  ARG   B CG  1 
ATOM   4256 C  CD  . ARG   B 1 258 ? 38.571 -27.476 -2.210  1.00 43.63  ? 951  ARG   B CD  1 
ATOM   4257 N  NE  . ARG   B 1 258 ? 37.366 -26.791 -2.682  1.00 46.52  ? 951  ARG   B NE  1 
ATOM   4258 C  CZ  . ARG   B 1 258 ? 36.825 -26.942 -3.884  1.00 47.93  ? 951  ARG   B CZ  1 
ATOM   4259 N  NH1 . ARG   B 1 258 ? 37.425 -27.686 -4.798  1.00 48.01  ? 951  ARG   B NH1 1 
ATOM   4260 N  NH2 . ARG   B 1 258 ? 35.707 -26.306 -4.198  1.00 47.74  ? 951  ARG   B NH2 1 
ATOM   4261 N  N   . LYS   B 1 259 ? 35.463 -27.224 1.514   1.00 38.50  ? 952  LYS   B N   1 
ATOM   4262 C  CA  . LYS   B 1 259 ? 34.006 -27.229 1.475   1.00 39.31  ? 952  LYS   B CA  1 
ATOM   4263 C  C   . LYS   B 1 259 ? 33.407 -25.828 1.650   1.00 40.63  ? 952  LYS   B C   1 
ATOM   4264 O  O   . LYS   B 1 259 ? 32.350 -25.547 1.097   1.00 41.39  ? 952  LYS   B O   1 
ATOM   4265 C  CB  . LYS   B 1 259 ? 33.440 -28.201 2.498   1.00 40.88  ? 952  LYS   B CB  1 
ATOM   4266 C  CG  . LYS   B 1 259 ? 33.727 -29.651 2.176   1.00 45.32  ? 952  LYS   B CG  1 
ATOM   4267 C  CD  . LYS   B 1 259 ? 32.923 -30.566 3.059   1.00 50.53  ? 952  LYS   B CD  1 
ATOM   4268 C  CE  . LYS   B 1 259 ? 31.444 -30.670 2.665   1.00 54.78  ? 952  LYS   B CE  1 
ATOM   4269 N  NZ  . LYS   B 1 259 ? 30.571 -29.500 3.078   1.00 55.70  ? 952  LYS   B NZ  1 
ATOM   4270 N  N   . CYS   B 1 260 ? 34.060 -24.949 2.415   1.00 40.71  ? 953  CYS   B N   1 
ATOM   4271 C  CA  . CYS   B 1 260 ? 33.596 -23.560 2.563   1.00 41.10  ? 953  CYS   B CA  1 
ATOM   4272 C  C   . CYS   B 1 260 ? 33.683 -22.825 1.205   1.00 41.15  ? 953  CYS   B C   1 
ATOM   4273 O  O   . CYS   B 1 260 ? 32.970 -21.852 0.983   1.00 41.05  ? 953  CYS   B O   1 
ATOM   4274 C  CB  . CYS   B 1 260 ? 34.412 -22.818 3.623   1.00 41.88  ? 953  CYS   B CB  1 
ATOM   4275 S  SG  . CYS   B 1 260 ? 34.339 -23.529 5.288   1.00 42.61  ? 953  CYS   B SG  1 
ATOM   4276 N  N   . TRP   B 1 261 ? 34.583 -23.277 0.317   1.00 40.80  ? 954  TRP   B N   1 
ATOM   4277 C  CA  . TRP   B 1 261 ? 34.835 -22.688 -0.978  1.00 40.35  ? 954  TRP   B CA  1 
ATOM   4278 C  C   . TRP   B 1 261 ? 34.079 -23.413 -2.082  1.00 41.10  ? 954  TRP   B C   1 
ATOM   4279 O  O   . TRP   B 1 261 ? 34.595 -23.544 -3.186  1.00 41.59  ? 954  TRP   B O   1 
ATOM   4280 C  CB  . TRP   B 1 261 ? 36.350 -22.684 -1.253  1.00 39.48  ? 954  TRP   B CB  1 
ATOM   4281 C  CG  . TRP   B 1 261 ? 37.171 -22.086 -0.145  1.00 39.07  ? 954  TRP   B CG  1 
ATOM   4282 C  CD1 . TRP   B 1 261 ? 36.830 -21.038 0.660   1.00 39.63  ? 954  TRP   B CD1 1 
ATOM   4283 C  CD2 . TRP   B 1 261 ? 38.478 -22.499 0.266   1.00 39.03  ? 954  TRP   B CD2 1 
ATOM   4284 N  NE1 . TRP   B 1 261 ? 37.835 -20.793 1.569   1.00 39.88  ? 954  TRP   B NE1 1 
ATOM   4285 C  CE2 . TRP   B 1 261 ? 38.864 -21.669 1.341   1.00 39.74  ? 954  TRP   B CE2 1 
ATOM   4286 C  CE3 . TRP   B 1 261 ? 39.358 -23.498 -0.161  1.00 39.75  ? 954  TRP   B CE3 1 
ATOM   4287 C  CZ2 . TRP   B 1 261 ? 40.103 -21.795 1.977   1.00 40.48  ? 954  TRP   B CZ2 1 
ATOM   4288 C  CZ3 . TRP   B 1 261 ? 40.574 -23.638 0.486   1.00 40.69  ? 954  TRP   B CZ3 1 
ATOM   4289 C  CH2 . TRP   B 1 261 ? 40.930 -22.802 1.551   1.00 40.74  ? 954  TRP   B CH2 1 
ATOM   4290 N  N   . MET   B 1 262 ? 32.860 -23.881 -1.802  1.00 41.37  ? 955  MET   B N   1 
ATOM   4291 C  CA  . MET   B 1 262 ? 32.051 -24.553 -2.823  1.00 42.07  ? 955  MET   B CA  1 
ATOM   4292 C  C   . MET   B 1 262 ? 31.332 -23.537 -3.715  1.00 43.19  ? 955  MET   B C   1 
ATOM   4293 O  O   . MET   B 1 262 ? 31.058 -22.434 -3.267  1.00 43.44  ? 955  MET   B O   1 
ATOM   4294 C  CB  . MET   B 1 262 ? 31.034 -25.491 -2.178  1.00 41.76  ? 955  MET   B CB  1 
ATOM   4295 C  CG  . MET   B 1 262 ? 31.603 -26.850 -1.842  1.00 42.88  ? 955  MET   B CG  1 
ATOM   4296 S  SD  . MET   B 1 262 ? 30.320 -27.946 -1.185  1.00 44.93  ? 955  MET   B SD  1 
ATOM   4297 C  CE  . MET   B 1 262 ? 31.242 -29.000 -0.391  1.00 44.41  ? 955  MET   B CE  1 
ATOM   4298 N  N   . ILE   B 1 263 ? 31.011 -23.899 -4.964  1.00 43.74  ? 956  ILE   B N   1 
ATOM   4299 C  CA  . ILE   B 1 263 ? 30.300 -22.991 -5.868  1.00 44.77  ? 956  ILE   B CA  1 
ATOM   4300 C  C   . ILE   B 1 263 ? 28.832 -22.866 -5.430  1.00 46.24  ? 956  ILE   B C   1 
ATOM   4301 O  O   . ILE   B 1 263 ? 28.314 -21.748 -5.374  1.00 46.83  ? 956  ILE   B O   1 
ATOM   4302 C  CB  . ILE   B 1 263 ? 30.458 -23.386 -7.363  1.00 44.94  ? 956  ILE   B CB  1 
ATOM   4303 C  CG1 . ILE   B 1 263 ? 31.938 -23.407 -7.808  1.00 45.55  ? 956  ILE   B CG1 1 
ATOM   4304 C  CG2 . ILE   B 1 263 ? 29.597 -22.505 -8.271  1.00 45.25  ? 956  ILE   B CG2 1 
ATOM   4305 C  CD1 . ILE   B 1 263 ? 32.595 -22.063 -7.954  1.00 46.88  ? 956  ILE   B CD1 1 
ATOM   4306 N  N   . ASP   B 1 264 ? 28.181 -23.985 -5.061  1.00 46.87  ? 957  ASP   B N   1 
ATOM   4307 C  CA  . ASP   B 1 264 ? 26.799 -23.911 -4.588  1.00 48.23  ? 957  ASP   B CA  1 
ATOM   4308 C  C   . ASP   B 1 264 ? 26.788 -23.501 -3.131  1.00 49.19  ? 957  ASP   B C   1 
ATOM   4309 O  O   . ASP   B 1 264 ? 27.190 -24.282 -2.262  1.00 49.57  ? 957  ASP   B O   1 
ATOM   4310 C  CB  . ASP   B 1 264 ? 26.008 -25.212 -4.782  1.00 50.20  ? 957  ASP   B CB  1 
ATOM   4311 C  CG  . ASP   B 1 264 ? 24.534 -25.025 -4.435  1.00 55.61  ? 957  ASP   B CG  1 
ATOM   4312 O  OD1 . ASP   B 1 264 ? 23.997 -23.919 -4.700  1.00 56.89  ? 957  ASP   B OD1 1 
ATOM   4313 O  OD2 . ASP   B 1 264 ? 23.926 -25.968 -3.866  1.00 57.51  ? 957  ASP   B OD2 1 
ATOM   4314 N  N   . ALA   B 1 265 ? 26.313 -22.272 -2.874  1.00 49.14  ? 958  ALA   B N   1 
ATOM   4315 C  CA  . ALA   B 1 265 ? 26.252 -21.670 -1.550  1.00 49.01  ? 958  ALA   B CA  1 
ATOM   4316 C  C   . ALA   B 1 265 ? 25.552 -22.522 -0.512  1.00 49.01  ? 958  ALA   B C   1 
ATOM   4317 O  O   . ALA   B 1 265 ? 26.076 -22.665 0.588   1.00 49.82  ? 958  ALA   B O   1 
ATOM   4318 C  CB  . ALA   B 1 265 ? 25.613 -20.295 -1.624  1.00 48.87  ? 958  ALA   B CB  1 
ATOM   4319 N  N   . ASP   B 1 266 ? 24.400 -23.117 -0.848  1.00 48.17  ? 959  ASP   B N   1 
ATOM   4320 C  CA  . ASP   B 1 266 ? 23.662 -23.934 0.118   1.00 47.64  ? 959  ASP   B CA  1 
ATOM   4321 C  C   . ASP   B 1 266 ? 24.339 -25.265 0.452   1.00 46.40  ? 959  ASP   B C   1 
ATOM   4322 O  O   . ASP   B 1 266 ? 24.018 -25.864 1.472   1.00 46.61  ? 959  ASP   B O   1 
ATOM   4323 C  CB  . ASP   B 1 266 ? 22.214 -24.143 -0.324  1.00 49.86  ? 959  ASP   B CB  1 
ATOM   4324 C  CG  . ASP   B 1 266 ? 21.443 -22.841 -0.408  1.00 56.47  ? 959  ASP   B CG  1 
ATOM   4325 O  OD1 . ASP   B 1 266 ? 21.756 -21.912 0.368   1.00 57.17  ? 959  ASP   B OD1 1 
ATOM   4326 O  OD2 . ASP   B 1 266 ? 20.533 -22.744 -1.255  1.00 60.34  ? 959  ASP   B OD2 1 
ATOM   4327 N  N   . SER   B 1 267 ? 25.277 -25.716 -0.374  1.00 45.36  ? 960  SER   B N   1 
ATOM   4328 C  CA  . SER   B 1 267 ? 25.998 -26.959 -0.114  1.00 45.01  ? 960  SER   B CA  1 
ATOM   4329 C  C   . SER   B 1 267 ? 27.162 -26.781 0.861   1.00 44.05  ? 960  SER   B C   1 
ATOM   4330 O  O   . SER   B 1 267 ? 27.690 -27.772 1.344   1.00 44.95  ? 960  SER   B O   1 
ATOM   4331 C  CB  . SER   B 1 267 ? 26.495 -27.573 -1.421  1.00 47.01  ? 960  SER   B CB  1 
ATOM   4332 O  OG  . SER   B 1 267 ? 25.431 -27.730 -2.345  1.00 49.95  ? 960  SER   B OG  1 
ATOM   4333 N  N   . ARG   B 1 268 ? 27.589 -25.545 1.127   1.00 42.63  ? 961  ARG   B N   1 
ATOM   4334 C  CA  . ARG   B 1 268 ? 28.689 -25.243 2.041   1.00 41.77  ? 961  ARG   B CA  1 
ATOM   4335 C  C   . ARG   B 1 268 ? 28.321 -25.603 3.488   1.00 41.05  ? 961  ARG   B C   1 
ATOM   4336 O  O   . ARG   B 1 268 ? 27.145 -25.543 3.874   1.00 40.51  ? 961  ARG   B O   1 
ATOM   4337 C  CB  . ARG   B 1 268 ? 29.026 -23.737 1.967   1.00 42.29  ? 961  ARG   B CB  1 
ATOM   4338 C  CG  . ARG   B 1 268 ? 29.687 -23.328 0.669   1.00 43.04  ? 961  ARG   B CG  1 
ATOM   4339 C  CD  . ARG   B 1 268 ? 29.762 -21.831 0.545   1.00 43.93  ? 961  ARG   B CD  1 
ATOM   4340 N  NE  . ARG   B 1 268 ? 30.000 -21.431 -0.840  1.00 46.08  ? 961  ARG   B NE  1 
ATOM   4341 C  CZ  . ARG   B 1 268 ? 29.593 -20.283 -1.372  1.00 48.10  ? 961  ARG   B CZ  1 
ATOM   4342 N  NH1 . ARG   B 1 268 ? 28.937 -19.398 -0.635  1.00 48.47  ? 961  ARG   B NH1 1 
ATOM   4343 N  NH2 . ARG   B 1 268 ? 29.839 -20.012 -2.645  1.00 47.60  ? 961  ARG   B NH2 1 
ATOM   4344 N  N   . PRO   B 1 269 ? 29.331 -25.942 4.313   1.00 40.56  ? 962  PRO   B N   1 
ATOM   4345 C  CA  . PRO   B 1 269 ? 29.045 -26.256 5.717   1.00 40.32  ? 962  PRO   B CA  1 
ATOM   4346 C  C   . PRO   B 1 269 ? 28.424 -25.076 6.458   1.00 40.92  ? 962  PRO   B C   1 
ATOM   4347 O  O   . PRO   B 1 269 ? 28.706 -23.926 6.127   1.00 41.54  ? 962  PRO   B O   1 
ATOM   4348 C  CB  . PRO   B 1 269 ? 30.417 -26.611 6.298   1.00 40.59  ? 962  PRO   B CB  1 
ATOM   4349 C  CG  . PRO   B 1 269 ? 31.411 -26.114 5.339   1.00 40.92  ? 962  PRO   B CG  1 
ATOM   4350 C  CD  . PRO   B 1 269 ? 30.766 -26.084 4.001   1.00 39.81  ? 962  PRO   B CD  1 
ATOM   4351 N  N   . LYS   B 1 270 ? 27.550 -25.351 7.432   1.00 40.52  ? 963  LYS   B N   1 
ATOM   4352 C  CA  . LYS   B 1 270 ? 26.929 -24.292 8.216   1.00 40.80  ? 963  LYS   B CA  1 
ATOM   4353 C  C   . LYS   B 1 270 ? 27.822 -23.941 9.401   1.00 40.65  ? 963  LYS   B C   1 
ATOM   4354 O  O   . LYS   B 1 270 ? 28.604 -24.789 9.831   1.00 40.90  ? 963  LYS   B O   1 
ATOM   4355 C  CB  . LYS   B 1 270 ? 25.546 -24.724 8.701   1.00 43.39  ? 963  LYS   B CB  1 
ATOM   4356 C  CG  . LYS   B 1 270 ? 24.418 -24.325 7.764   1.00 49.24  ? 963  LYS   B CG  1 
ATOM   4357 C  CD  . LYS   B 1 270 ? 24.463 -25.138 6.477   1.00 56.53  ? 963  LYS   B CD  1 
ATOM   4358 C  CE  . LYS   B 1 270 ? 23.800 -24.452 5.317   1.00 61.64  ? 963  LYS   B CE  1 
ATOM   4359 N  NZ  . LYS   B 1 270 ? 22.538 -23.781 5.745   1.00 65.10  ? 963  LYS   B NZ  1 
ATOM   4360 N  N   . PHE   B 1 271 ? 27.703 -22.722 9.955   1.00 40.20  ? 964  PHE   B N   1 
ATOM   4361 C  CA  . PHE   B 1 271 ? 28.519 -22.347 11.121  1.00 40.50  ? 964  PHE   B CA  1 
ATOM   4362 C  C   . PHE   B 1 271 ? 28.264 -23.258 12.307  1.00 40.76  ? 964  PHE   B C   1 
ATOM   4363 O  O   . PHE   B 1 271 ? 29.196 -23.530 13.054  1.00 40.36  ? 964  PHE   B O   1 
ATOM   4364 C  CB  . PHE   B 1 271 ? 28.328 -20.880 11.520  1.00 40.33  ? 964  PHE   B CB  1 
ATOM   4365 C  CG  . PHE   B 1 271 ? 28.942 -19.900 10.557  1.00 40.63  ? 964  PHE   B CG  1 
ATOM   4366 C  CD1 . PHE   B 1 271 ? 30.313 -19.871 10.353  1.00 41.44  ? 964  PHE   B CD1 1 
ATOM   4367 C  CD2 . PHE   B 1 271 ? 28.152 -19.017 9.850   1.00 40.93  ? 964  PHE   B CD2 1 
ATOM   4368 C  CE1 . PHE   B 1 271 ? 30.878 -18.981 9.454   1.00 41.93  ? 964  PHE   B CE1 1 
ATOM   4369 C  CE2 . PHE   B 1 271 ? 28.717 -18.137 8.945   1.00 41.74  ? 964  PHE   B CE2 1 
ATOM   4370 C  CZ  . PHE   B 1 271 ? 30.079 -18.116 8.760   1.00 41.65  ? 964  PHE   B CZ  1 
ATOM   4371 N  N   . ARG   B 1 272 ? 27.025 -23.776 12.436  1.00 41.48  ? 965  ARG   B N   1 
ATOM   4372 C  CA  . ARG   B 1 272 ? 26.580 -24.709 13.476  1.00 42.92  ? 965  ARG   B CA  1 
ATOM   4373 C  C   . ARG   B 1 272 ? 27.404 -25.998 13.371  1.00 42.79  ? 965  ARG   B C   1 
ATOM   4374 O  O   . ARG   B 1 272 ? 27.926 -26.474 14.371  1.00 42.78  ? 965  ARG   B O   1 
ATOM   4375 C  CB  . ARG   B 1 272 ? 25.091 -25.017 13.251  1.00 46.79  ? 965  ARG   B CB  1 
ATOM   4376 C  CG  . ARG   B 1 272 ? 24.284 -25.259 14.504  1.00 55.92  ? 965  ARG   B CG  1 
ATOM   4377 C  CD  . ARG   B 1 272 ? 23.893 -26.728 14.650  1.00 64.57  ? 965  ARG   B CD  1 
ATOM   4378 N  NE  . ARG   B 1 272 ? 22.490 -26.955 14.273  1.00 72.20  ? 965  ARG   B NE  1 
ATOM   4379 C  CZ  . ARG   B 1 272 ? 21.453 -26.803 15.105  1.00 77.29  ? 965  ARG   B CZ  1 
ATOM   4380 N  NH1 . ARG   B 1 272 ? 21.652 -26.412 16.363  1.00 77.08  ? 965  ARG   B NH1 1 
ATOM   4381 N  NH2 . ARG   B 1 272 ? 20.208 -27.021 14.677  1.00 77.90  ? 965  ARG   B NH2 1 
ATOM   4382 N  N   . GLU   B 1 273 ? 27.557 -26.532 12.142  1.00 42.63  ? 966  GLU   B N   1 
ATOM   4383 C  CA  . GLU   B 1 273 ? 28.310 -27.742 11.836  1.00 42.83  ? 966  GLU   B CA  1 
ATOM   4384 C  C   . GLU   B 1 273 ? 29.813 -27.527 12.017  1.00 42.70  ? 966  GLU   B C   1 
ATOM   4385 O  O   . GLU   B 1 273 ? 30.522 -28.448 12.437  1.00 43.23  ? 966  GLU   B O   1 
ATOM   4386 C  CB  . GLU   B 1 273 ? 28.038 -28.161 10.387  1.00 45.08  ? 966  GLU   B CB  1 
ATOM   4387 C  CG  . GLU   B 1 273 ? 26.577 -28.412 10.080  1.00 49.98  ? 966  GLU   B CG  1 
ATOM   4388 C  CD  . GLU   B 1 273 ? 26.248 -28.563 8.608   1.00 57.53  ? 966  GLU   B CD  1 
ATOM   4389 O  OE1 . GLU   B 1 273 ? 25.054 -28.781 8.299   1.00 60.45  ? 966  GLU   B OE1 1 
ATOM   4390 O  OE2 . GLU   B 1 273 ? 27.164 -28.437 7.761   1.00 58.29  ? 966  GLU   B OE2 1 
ATOM   4391 N  N   . LEU   B 1 274 ? 30.301 -26.331 11.662  1.00 41.60  ? 967  LEU   B N   1 
ATOM   4392 C  CA  . LEU   B 1 274 ? 31.711 -25.973 11.778  1.00 41.19  ? 967  LEU   B CA  1 
ATOM   4393 C  C   . LEU   B 1 274 ? 32.154 -25.939 13.249  1.00 40.84  ? 967  LEU   B C   1 
ATOM   4394 O  O   . LEU   B 1 274 ? 33.268 -26.353 13.566  1.00 40.62  ? 967  LEU   B O   1 
ATOM   4395 C  CB  . LEU   B 1 274 ? 31.980 -24.621 11.084  1.00 41.13  ? 967  LEU   B CB  1 
ATOM   4396 C  CG  . LEU   B 1 274 ? 31.808 -24.603 9.563   1.00 41.87  ? 967  LEU   B CG  1 
ATOM   4397 C  CD1 . LEU   B 1 274 ? 31.768 -23.193 9.035   1.00 42.17  ? 967  LEU   B CD1 1 
ATOM   4398 C  CD2 . LEU   B 1 274 ? 32.885 -25.397 8.878   1.00 42.20  ? 967  LEU   B CD2 1 
ATOM   4399 N  N   . ILE   B 1 275 ? 31.268 -25.483 14.150  1.00 40.40  ? 968  ILE   B N   1 
ATOM   4400 C  CA  . ILE   B 1 275 ? 31.543 -25.451 15.587  1.00 40.05  ? 968  ILE   B CA  1 
ATOM   4401 C  C   . ILE   B 1 275 ? 31.732 -26.876 16.079  1.00 41.00  ? 968  ILE   B C   1 
ATOM   4402 O  O   . ILE   B 1 275 ? 32.687 -27.143 16.795  1.00 41.52  ? 968  ILE   B O   1 
ATOM   4403 C  CB  . ILE   B 1 275 ? 30.412 -24.758 16.394  1.00 39.37  ? 968  ILE   B CB  1 
ATOM   4404 C  CG1 . ILE   B 1 275 ? 30.238 -23.296 16.009  1.00 39.54  ? 968  ILE   B CG1 1 
ATOM   4405 C  CG2 . ILE   B 1 275 ? 30.657 -24.883 17.891  1.00 39.77  ? 968  ILE   B CG2 1 
ATOM   4406 C  CD1 . ILE   B 1 275 ? 28.922 -22.708 16.504  1.00 40.47  ? 968  ILE   B CD1 1 
ATOM   4407 N  N   . ILE   B 1 276 ? 30.852 -27.796 15.661  1.00 40.84  ? 969  ILE   B N   1 
ATOM   4408 C  CA  . ILE   B 1 276 ? 30.928 -29.190 16.069  1.00 41.20  ? 969  ILE   B CA  1 
ATOM   4409 C  C   . ILE   B 1 276 ? 32.181 -29.892 15.526  1.00 41.46  ? 969  ILE   B C   1 
ATOM   4410 O  O   . ILE   B 1 276 ? 32.906 -30.518 16.301  1.00 41.46  ? 969  ILE   B O   1 
ATOM   4411 C  CB  . ILE   B 1 276 ? 29.612 -29.914 15.696  1.00 41.67  ? 969  ILE   B CB  1 
ATOM   4412 C  CG1 . ILE   B 1 276 ? 28.418 -29.288 16.470  1.00 42.69  ? 969  ILE   B CG1 1 
ATOM   4413 C  CG2 . ILE   B 1 276 ? 29.707 -31.423 15.949  1.00 41.59  ? 969  ILE   B CG2 1 
ATOM   4414 C  CD1 . ILE   B 1 276 ? 27.054 -29.520 15.847  1.00 43.79  ? 969  ILE   B CD1 1 
ATOM   4415 N  N   . GLU   B 1 277 ? 32.464 -29.756 14.223  1.00 41.45  ? 970  GLU   B N   1 
ATOM   4416 C  CA  . GLU   B 1 277 ? 33.634 -30.394 13.634  1.00 42.22  ? 970  GLU   B CA  1 
ATOM   4417 C  C   . GLU   B 1 277 ? 34.933 -29.922 14.275  1.00 41.74  ? 970  GLU   B C   1 
ATOM   4418 O  O   . GLU   B 1 277 ? 35.748 -30.753 14.671  1.00 42.23  ? 970  GLU   B O   1 
ATOM   4419 C  CB  . GLU   B 1 277 ? 33.685 -30.189 12.109  1.00 46.46  ? 970  GLU   B CB  1 
ATOM   4420 C  CG  . GLU   B 1 277 ? 33.310 -31.424 11.308  1.00 54.60  ? 970  GLU   B CG  1 
ATOM   4421 C  CD  . GLU   B 1 277 ? 34.103 -32.680 11.617  1.00 65.54  ? 970  GLU   B CD  1 
ATOM   4422 O  OE1 . GLU   B 1 277 ? 35.306 -32.729 11.268  1.00 68.69  ? 970  GLU   B OE1 1 
ATOM   4423 O  OE2 . GLU   B 1 277 ? 33.512 -33.628 12.187  1.00 68.38  ? 970  GLU   B OE2 1 
ATOM   4424 N  N   . PHE   B 1 278 ? 35.125 -28.606 14.391  1.00 40.86  ? 971  PHE   B N   1 
ATOM   4425 C  CA  . PHE   B 1 278 ? 36.343 -28.063 14.976  1.00 40.86  ? 971  PHE   B CA  1 
ATOM   4426 C  C   . PHE   B 1 278 ? 36.440 -28.329 16.486  1.00 41.67  ? 971  PHE   B C   1 
ATOM   4427 O  O   . PHE   B 1 278 ? 37.545 -28.380 17.014  1.00 41.67  ? 971  PHE   B O   1 
ATOM   4428 C  CB  . PHE   B 1 278 ? 36.517 -26.573 14.638  1.00 40.15  ? 971  PHE   B CB  1 
ATOM   4429 C  CG  . PHE   B 1 278 ? 37.056 -26.311 13.249  1.00 40.26  ? 971  PHE   B CG  1 
ATOM   4430 C  CD1 . PHE   B 1 278 ? 38.366 -26.613 12.928  1.00 40.75  ? 971  PHE   B CD1 1 
ATOM   4431 C  CD2 . PHE   B 1 278 ? 36.259 -25.739 12.273  1.00 40.63  ? 971  PHE   B CD2 1 
ATOM   4432 C  CE1 . PHE   B 1 278 ? 38.860 -26.361 11.654  1.00 40.98  ? 971  PHE   B CE1 1 
ATOM   4433 C  CE2 . PHE   B 1 278 ? 36.758 -25.490 11.000  1.00 40.95  ? 971  PHE   B CE2 1 
ATOM   4434 C  CZ  . PHE   B 1 278 ? 38.053 -25.801 10.699  1.00 40.54  ? 971  PHE   B CZ  1 
ATOM   4435 N  N   . SER   B 1 279 ? 35.299 -28.524 17.178  1.00 42.03  ? 972  SER   B N   1 
ATOM   4436 C  CA  . SER   B 1 279 ? 35.299 -28.862 18.603  1.00 42.98  ? 972  SER   B CA  1 
ATOM   4437 C  C   . SER   B 1 279 ? 35.770 -30.299 18.782  1.00 43.18  ? 972  SER   B C   1 
ATOM   4438 O  O   . SER   B 1 279 ? 36.579 -30.563 19.663  1.00 43.32  ? 972  SER   B O   1 
ATOM   4439 C  CB  . SER   B 1 279 ? 33.913 -28.691 19.213  1.00 45.08  ? 972  SER   B CB  1 
ATOM   4440 O  OG  . SER   B 1 279 ? 33.555 -27.322 19.231  1.00 48.82  ? 972  SER   B OG  1 
ATOM   4441 N  N   . LYS   B 1 280 ? 35.308 -31.219 17.915  1.00 43.17  ? 973  LYS   B N   1 
ATOM   4442 C  CA  . LYS   B 1 280 ? 35.729 -32.622 17.901  1.00 43.30  ? 973  LYS   B CA  1 
ATOM   4443 C  C   . LYS   B 1 280 ? 37.249 -32.665 17.645  1.00 43.22  ? 973  LYS   B C   1 
ATOM   4444 O  O   . LYS   B 1 280 ? 37.978 -33.328 18.373  1.00 43.52  ? 973  LYS   B O   1 
ATOM   4445 C  CB  . LYS   B 1 280 ? 34.944 -33.383 16.805  1.00 44.98  ? 973  LYS   B CB  1 
ATOM   4446 C  CG  . LYS   B 1 280 ? 35.539 -34.713 16.341  1.00 49.24  ? 973  LYS   B CG  1 
ATOM   4447 C  CD  . LYS   B 1 280 ? 35.208 -34.965 14.853  1.00 54.84  ? 973  LYS   B CD  1 
ATOM   4448 C  CE  . LYS   B 1 280 ? 35.954 -36.115 14.204  1.00 59.42  ? 973  LYS   B CE  1 
ATOM   4449 N  NZ  . LYS   B 1 280 ? 35.510 -37.451 14.708  1.00 61.73  ? 973  LYS   B NZ  1 
ATOM   4450 N  N   . MET   B 1 281 ? 37.725 -31.882 16.671  1.00 42.62  ? 974  MET   B N   1 
ATOM   4451 C  CA  . MET   B 1 281 ? 39.138 -31.801 16.357  1.00 42.57  ? 974  MET   B CA  1 
ATOM   4452 C  C   . MET   B 1 281 ? 39.977 -31.226 17.487  1.00 43.33  ? 974  MET   B C   1 
ATOM   4453 O  O   . MET   B 1 281 ? 41.076 -31.704 17.716  1.00 43.21  ? 974  MET   B O   1 
ATOM   4454 C  CB  . MET   B 1 281 ? 39.359 -31.015 15.071  1.00 42.69  ? 974  MET   B CB  1 
ATOM   4455 C  CG  . MET   B 1 281 ? 38.877 -31.740 13.850  1.00 44.59  ? 974  MET   B CG  1 
ATOM   4456 S  SD  . MET   B 1 281 ? 39.188 -30.787 12.343  1.00 46.64  ? 974  MET   B SD  1 
ATOM   4457 C  CE  . MET   B 1 281 ? 38.752 -31.973 11.147  1.00 49.40  ? 974  MET   B CE  1 
ATOM   4458 N  N   . ALA   B 1 282 ? 39.475 -30.208 18.203  1.00 44.24  ? 975  ALA   B N   1 
ATOM   4459 C  CA  . ALA   B 1 282 ? 40.233 -29.596 19.303  1.00 45.15  ? 975  ALA   B CA  1 
ATOM   4460 C  C   . ALA   B 1 282 ? 40.339 -30.470 20.558  1.00 46.52  ? 975  ALA   B C   1 
ATOM   4461 O  O   . ALA   B 1 282 ? 41.032 -30.091 21.498  1.00 46.74  ? 975  ALA   B O   1 
ATOM   4462 C  CB  . ALA   B 1 282 ? 39.678 -28.227 19.646  1.00 44.82  ? 975  ALA   B CB  1 
ATOM   4463 N  N   . ARG   B 1 283 ? 39.677 -31.634 20.579  1.00 47.24  ? 976  ARG   B N   1 
ATOM   4464 C  CA  . ARG   B 1 283 ? 39.790 -32.559 21.701  1.00 48.56  ? 976  ARG   B CA  1 
ATOM   4465 C  C   . ARG   B 1 283 ? 41.022 -33.470 21.559  1.00 50.47  ? 976  ARG   B C   1 
ATOM   4466 O  O   . ARG   B 1 283 ? 41.586 -33.895 22.564  1.00 50.97  ? 976  ARG   B O   1 
ATOM   4467 C  CB  . ARG   B 1 283 ? 38.496 -33.343 21.913  1.00 49.36  ? 976  ARG   B CB  1 
ATOM   4468 C  CG  . ARG   B 1 283 ? 37.366 -32.422 22.353  1.00 51.19  ? 976  ARG   B CG  1 
ATOM   4469 C  CD  . ARG   B 1 283 ? 36.213 -33.154 22.994  1.00 53.04  ? 976  ARG   B CD  1 
ATOM   4470 N  NE  . ARG   B 1 283 ? 35.373 -33.851 22.020  1.00 55.15  ? 976  ARG   B NE  1 
ATOM   4471 C  CZ  . ARG   B 1 283 ? 34.369 -33.283 21.360  1.00 56.96  ? 976  ARG   B CZ  1 
ATOM   4472 N  NH1 . ARG   B 1 283 ? 33.633 -33.997 20.519  1.00 56.83  ? 976  ARG   B NH1 1 
ATOM   4473 N  NH2 . ARG   B 1 283 ? 34.093 -31.997 21.535  1.00 56.27  ? 976  ARG   B NH2 1 
ATOM   4474 N  N   . ASP   B 1 284 ? 41.467 -33.724 20.316  1.00 51.43  ? 977  ASP   B N   1 
ATOM   4475 C  CA  . ASP   B 1 284 ? 42.688 -34.471 20.005  1.00 52.76  ? 977  ASP   B CA  1 
ATOM   4476 C  C   . ASP   B 1 284 ? 43.433 -33.606 18.974  1.00 54.06  ? 977  ASP   B C   1 
ATOM   4477 O  O   . ASP   B 1 284 ? 43.437 -33.928 17.780  1.00 54.35  ? 977  ASP   B O   1 
ATOM   4478 C  CB  . ASP   B 1 284 ? 42.344 -35.853 19.414  1.00 53.88  ? 977  ASP   B CB  1 
ATOM   4479 C  CG  . ASP   B 1 284 ? 43.450 -36.879 19.522  1.00 57.52  ? 977  ASP   B CG  1 
ATOM   4480 O  OD1 . ASP   B 1 284 ? 44.601 -36.488 19.853  1.00 58.17  ? 977  ASP   B OD1 1 
ATOM   4481 O  OD2 . ASP   B 1 284 ? 43.170 -38.076 19.275  1.00 59.58  ? 977  ASP   B OD2 1 
ATOM   4482 N  N   . PRO   B 1 285 ? 43.983 -32.450 19.413  1.00 54.38  ? 978  PRO   B N   1 
ATOM   4483 C  CA  . PRO   B 1 285 ? 44.589 -31.513 18.463  1.00 54.87  ? 978  PRO   B CA  1 
ATOM   4484 C  C   . PRO   B 1 285 ? 45.728 -32.036 17.605  1.00 55.99  ? 978  PRO   B C   1 
ATOM   4485 O  O   . PRO   B 1 285 ? 45.769 -31.699 16.423  1.00 56.44  ? 978  PRO   B O   1 
ATOM   4486 C  CB  . PRO   B 1 285 ? 45.062 -30.361 19.357  1.00 55.36  ? 978  PRO   B CB  1 
ATOM   4487 C  CG  . PRO   B 1 285 ? 44.246 -30.445 20.560  1.00 55.74  ? 978  PRO   B CG  1 
ATOM   4488 C  CD  . PRO   B 1 285 ? 44.009 -31.903 20.781  1.00 54.01  ? 978  PRO   B CD  1 
ATOM   4489 N  N   . GLN   B 1 286 ? 46.665 -32.817 18.180  1.00 56.19  ? 979  GLN   B N   1 
ATOM   4490 C  CA  . GLN   B 1 286 ? 47.801 -33.307 17.401  1.00 56.99  ? 979  GLN   B CA  1 
ATOM   4491 C  C   . GLN   B 1 286 ? 47.423 -34.302 16.307  1.00 57.41  ? 979  GLN   B C   1 
ATOM   4492 O  O   . GLN   B 1 286 ? 48.216 -34.538 15.393  1.00 57.43  ? 979  GLN   B O   1 
ATOM   4493 C  CB  . GLN   B 1 286 ? 48.898 -33.876 18.298  1.00 59.30  ? 979  GLN   B CB  1 
ATOM   4494 C  CG  . GLN   B 1 286 ? 49.800 -32.807 18.884  1.00 65.10  ? 979  GLN   B CG  1 
ATOM   4495 C  CD  . GLN   B 1 286 ? 49.576 -32.699 20.364  1.00 73.02  ? 979  GLN   B CD  1 
ATOM   4496 O  OE1 . GLN   B 1 286 ? 48.527 -32.220 20.834  1.00 75.08  ? 979  GLN   B OE1 1 
ATOM   4497 N  NE2 . GLN   B 1 286 ? 50.555 -33.165 21.134  1.00 74.96  ? 979  GLN   B NE2 1 
ATOM   4498 N  N   . ARG   B 1 287 ? 46.223 -34.883 16.388  1.00 57.40  ? 980  ARG   B N   1 
ATOM   4499 C  CA  . ARG   B 1 287 ? 45.732 -35.800 15.376  1.00 57.73  ? 980  ARG   B CA  1 
ATOM   4500 C  C   . ARG   B 1 287 ? 45.264 -35.034 14.094  1.00 57.71  ? 980  ARG   B C   1 
ATOM   4501 O  O   . ARG   B 1 287 ? 45.271 -35.604 13.003  1.00 57.78  ? 980  ARG   B O   1 
ATOM   4502 C  CB  . ARG   B 1 287 ? 44.640 -36.700 15.999  1.00 59.34  ? 980  ARG   B CB  1 
ATOM   4503 C  CG  . ARG   B 1 287 ? 43.575 -37.198 15.052  1.00 63.82  ? 980  ARG   B CG  1 
ATOM   4504 C  CD  . ARG   B 1 287 ? 42.986 -38.523 15.463  1.00 69.67  ? 980  ARG   B CD  1 
ATOM   4505 N  NE  . ARG   B 1 287 ? 41.798 -38.827 14.663  1.00 75.65  ? 980  ARG   B NE  1 
ATOM   4506 C  CZ  . ARG   B 1 287 ? 41.826 -39.365 13.444  1.00 79.40  ? 980  ARG   B CZ  1 
ATOM   4507 N  NH1 . ARG   B 1 287 ? 40.695 -39.586 12.782  1.00 79.23  ? 980  ARG   B NH1 1 
ATOM   4508 N  NH2 . ARG   B 1 287 ? 42.986 -39.665 12.869  1.00 79.74  ? 980  ARG   B NH2 1 
ATOM   4509 N  N   . TYR   B 1 288 ? 44.909 -33.741 14.218  1.00 57.40  ? 981  TYR   B N   1 
ATOM   4510 C  CA  . TYR   B 1 288 ? 44.422 -32.967 13.088  1.00 57.61  ? 981  TYR   B CA  1 
ATOM   4511 C  C   . TYR   B 1 288 ? 45.396 -31.905 12.577  1.00 58.61  ? 981  TYR   B C   1 
ATOM   4512 O  O   . TYR   B 1 288 ? 45.346 -31.566 11.393  1.00 58.83  ? 981  TYR   B O   1 
ATOM   4513 C  CB  . TYR   B 1 288 ? 43.061 -32.378 13.424  1.00 57.19  ? 981  TYR   B CB  1 
ATOM   4514 C  CG  . TYR   B 1 288 ? 42.064 -33.489 13.640  1.00 57.36  ? 981  TYR   B CG  1 
ATOM   4515 C  CD1 . TYR   B 1 288 ? 41.614 -34.257 12.576  1.00 58.26  ? 981  TYR   B CD1 1 
ATOM   4516 C  CD2 . TYR   B 1 288 ? 41.676 -33.861 14.918  1.00 58.00  ? 981  TYR   B CD2 1 
ATOM   4517 C  CE1 . TYR   B 1 288 ? 40.740 -35.319 12.771  1.00 59.15  ? 981  TYR   B CE1 1 
ATOM   4518 C  CE2 . TYR   B 1 288 ? 40.787 -34.908 15.127  1.00 58.86  ? 981  TYR   B CE2 1 
ATOM   4519 C  CZ  . TYR   B 1 288 ? 40.321 -35.638 14.048  1.00 59.74  ? 981  TYR   B CZ  1 
ATOM   4520 O  OH  . TYR   B 1 288 ? 39.451 -36.684 14.237  1.00 60.61  ? 981  TYR   B OH  1 
ATOM   4521 N  N   . LEU   B 1 289 ? 46.296 -31.410 13.426  1.00 59.34  ? 982  LEU   B N   1 
ATOM   4522 C  CA  . LEU   B 1 289 ? 47.299 -30.451 12.973  1.00 60.95  ? 982  LEU   B CA  1 
ATOM   4523 C  C   . LEU   B 1 289 ? 48.685 -30.952 13.337  1.00 62.90  ? 982  LEU   B C   1 
ATOM   4524 O  O   . LEU   B 1 289 ? 48.938 -31.321 14.492  1.00 63.25  ? 982  LEU   B O   1 
ATOM   4525 C  CB  . LEU   B 1 289 ? 47.072 -29.032 13.511  1.00 61.21  ? 982  LEU   B CB  1 
ATOM   4526 C  CG  . LEU   B 1 289 ? 45.859 -28.272 12.993  1.00 63.02  ? 982  LEU   B CG  1 
ATOM   4527 C  CD1 . LEU   B 1 289 ? 45.826 -26.876 13.575  1.00 63.54  ? 982  LEU   B CD1 1 
ATOM   4528 C  CD2 . LEU   B 1 289 ? 45.856 -28.186 11.470  1.00 64.00  ? 982  LEU   B CD2 1 
ATOM   4529 N  N   . VAL   B 1 290 ? 49.578 -30.982 12.344  1.00 63.84  ? 983  VAL   B N   1 
ATOM   4530 C  CA  . VAL   B 1 290 ? 50.942 -31.444 12.520  1.00 65.43  ? 983  VAL   B CA  1 
ATOM   4531 C  C   . VAL   B 1 290 ? 51.882 -30.251 12.554  1.00 66.73  ? 983  VAL   B C   1 
ATOM   4532 O  O   . VAL   B 1 290 ? 52.258 -29.723 11.512  1.00 66.68  ? 983  VAL   B O   1 
ATOM   4533 C  CB  . VAL   B 1 290 ? 51.335 -32.467 11.430  1.00 66.64  ? 983  VAL   B CB  1 
ATOM   4534 C  CG1 . VAL   B 1 290 ? 52.717 -33.048 11.711  1.00 67.58  ? 983  VAL   B CG1 1 
ATOM   4535 C  CG2 . VAL   B 1 290 ? 50.294 -33.585 11.319  1.00 66.95  ? 983  VAL   B CG2 1 
ATOM   4536 N  N   . ILE   B 1 291 ? 52.231 -29.805 13.763  1.00 67.95  ? 984  ILE   B N   1 
ATOM   4537 C  CA  . ILE   B 1 291 ? 53.106 -28.655 13.989  1.00 69.82  ? 984  ILE   B CA  1 
ATOM   4538 C  C   . ILE   B 1 291 ? 54.354 -29.112 14.748  1.00 72.49  ? 984  ILE   B C   1 
ATOM   4539 O  O   . ILE   B 1 291 ? 54.236 -29.873 15.707  1.00 72.82  ? 984  ILE   B O   1 
ATOM   4540 C  CB  . ILE   B 1 291 ? 52.327 -27.561 14.778  1.00 69.68  ? 984  ILE   B CB  1 
ATOM   4541 C  CG1 . ILE   B 1 291 ? 51.130 -27.057 13.979  1.00 70.13  ? 984  ILE   B CG1 1 
ATOM   4542 C  CG2 . ILE   B 1 291 ? 53.225 -26.408 15.205  1.00 70.10  ? 984  ILE   B CG2 1 
ATOM   4543 C  CD1 . ILE   B 1 291 ? 50.154 -26.400 14.773  1.00 71.00  ? 984  ILE   B CD1 1 
ATOM   4544 N  N   . GLN   B 1 292 ? 55.544 -28.676 14.312  1.00 74.33  ? 985  GLN   B N   1 
ATOM   4545 C  CA  . GLN   B 1 292 ? 56.795 -29.052 14.968  1.00 76.65  ? 985  GLN   B CA  1 
ATOM   4546 C  C   . GLN   B 1 292 ? 56.871 -28.462 16.377  1.00 78.35  ? 985  GLN   B C   1 
ATOM   4547 O  O   . GLN   B 1 292 ? 56.755 -27.250 16.550  1.00 78.77  ? 985  GLN   B O   1 
ATOM   4548 C  CB  . GLN   B 1 292 ? 57.999 -28.616 14.117  1.00 79.13  ? 985  GLN   B CB  1 
ATOM   4549 C  CG  . GLN   B 1 292 ? 57.960 -29.164 12.686  1.00 83.98  ? 985  GLN   B CG  1 
ATOM   4550 C  CD  . GLN   B 1 292 ? 58.341 -30.630 12.600  1.00 89.80  ? 985  GLN   B CD  1 
ATOM   4551 O  OE1 . GLN   B 1 292 ? 59.510 -30.984 12.373  1.00 91.60  ? 985  GLN   B OE1 1 
ATOM   4552 N  NE2 . GLN   B 1 292 ? 57.362 -31.520 12.761  1.00 90.69  ? 985  GLN   B NE2 1 
ATOM   4553 N  N   . GLY   B 1 293 ? 57.023 -29.331 17.371  1.00 79.11  ? 986  GLY   B N   1 
ATOM   4554 C  CA  . GLY   B 1 293 ? 57.083 -28.922 18.769  1.00 80.07  ? 986  GLY   B CA  1 
ATOM   4555 C  C   . GLY   B 1 293 ? 55.724 -28.934 19.435  1.00 80.95  ? 986  GLY   B C   1 
ATOM   4556 O  O   . GLY   B 1 293 ? 55.311 -27.933 20.019  1.00 81.04  ? 986  GLY   B O   1 
ATOM   4557 N  N   . ASP   B 1 294 ? 55.013 -30.062 19.342  1.00 81.36  ? 987  ASP   B N   1 
ATOM   4558 C  CA  . ASP   B 1 294 ? 53.688 -30.193 19.944  1.00 82.14  ? 987  ASP   B CA  1 
ATOM   4559 C  C   . ASP   B 1 294 ? 53.593 -31.416 20.866  1.00 82.53  ? 987  ASP   B C   1 
ATOM   4560 O  O   . ASP   B 1 294 ? 54.488 -32.259 20.895  1.00 82.63  ? 987  ASP   B O   1 
ATOM   4561 C  CB  . ASP   B 1 294 ? 52.594 -30.241 18.856  1.00 83.72  ? 987  ASP   B CB  1 
ATOM   4562 C  CG  . ASP   B 1 294 ? 51.633 -29.061 18.861  1.00 87.33  ? 987  ASP   B CG  1 
ATOM   4563 O  OD1 . ASP   B 1 294 ? 51.882 -28.091 19.610  1.00 87.88  ? 987  ASP   B OD1 1 
ATOM   4564 O  OD2 . ASP   B 1 294 ? 50.634 -29.109 18.115  1.00 89.11  ? 987  ASP   B OD2 1 
ATOM   4565 N  N   . MET   C 1 312 ? 44.450 -18.955 38.126  1.00 76.57  ? 1005 MET   D N   1 
ATOM   4566 C  CA  . MET   C 1 312 ? 45.260 -18.521 36.981  1.00 76.93  ? 1005 MET   D CA  1 
ATOM   4567 C  C   . MET   C 1 312 ? 44.671 -17.318 36.238  1.00 76.51  ? 1005 MET   D C   1 
ATOM   4568 O  O   . MET   C 1 312 ? 45.416 -16.594 35.566  1.00 76.53  ? 1005 MET   D O   1 
ATOM   4569 C  CB  . MET   C 1 312 ? 45.453 -19.671 35.978  1.00 77.78  ? 1005 MET   D CB  1 
ATOM   4570 C  CG  . MET   C 1 312 ? 46.603 -20.575 36.315  1.00 80.56  ? 1005 MET   D CG  1 
ATOM   4571 S  SD  . MET   C 1 312 ? 47.137 -21.567 34.899  1.00 87.46  ? 1005 MET   D SD  1 
ATOM   4572 C  CE  . MET   C 1 312 ? 45.640 -22.496 34.559  1.00 87.29  ? 1005 MET   D CE  1 
ATOM   4573 N  N   . ASP   C 1 313 ? 43.329 -17.144 36.317  1.00 75.67  ? 1006 ASP   D N   1 
ATOM   4574 C  CA  . ASP   C 1 313 ? 42.569 -16.108 35.593  1.00 75.07  ? 1006 ASP   D CA  1 
ATOM   4575 C  C   . ASP   C 1 313 ? 42.591 -16.358 34.052  1.00 72.78  ? 1006 ASP   D C   1 
ATOM   4576 O  O   . ASP   C 1 313 ? 42.357 -15.437 33.270  1.00 73.01  ? 1006 ASP   D O   1 
ATOM   4577 C  CB  . ASP   C 1 313 ? 43.036 -14.678 35.961  1.00 77.92  ? 1006 ASP   D CB  1 
ATOM   4578 C  CG  . ASP   C 1 313 ? 41.973 -13.602 35.811  1.00 83.72  ? 1006 ASP   D CG  1 
ATOM   4579 O  OD1 . ASP   C 1 313 ? 40.822 -13.834 36.261  1.00 85.10  ? 1006 ASP   D OD1 1 
ATOM   4580 O  OD2 . ASP   C 1 313 ? 42.295 -12.519 35.258  1.00 85.50  ? 1006 ASP   D OD2 1 
ATOM   4581 N  N   . GLU   C 1 314 ? 42.857 -17.620 33.640  1.00 70.34  ? 1007 GLU   D N   1 
ATOM   4582 C  CA  . GLU   C 1 314 ? 42.912 -18.083 32.255  1.00 68.31  ? 1007 GLU   D CA  1 
ATOM   4583 C  C   . GLU   C 1 314 ? 41.513 -18.525 31.825  1.00 65.53  ? 1007 GLU   D C   1 
ATOM   4584 O  O   . GLU   C 1 314 ? 40.829 -19.217 32.582  1.00 65.71  ? 1007 GLU   D O   1 
ATOM   4585 C  CB  . GLU   C 1 314 ? 43.853 -19.294 32.162  1.00 70.15  ? 1007 GLU   D CB  1 
ATOM   4586 C  CG  . GLU   C 1 314 ? 45.119 -19.057 31.363  1.00 73.91  ? 1007 GLU   D CG  1 
ATOM   4587 C  CD  . GLU   C 1 314 ? 45.660 -20.315 30.708  1.00 79.78  ? 1007 GLU   D CD  1 
ATOM   4588 O  OE1 . GLU   C 1 314 ? 44.863 -21.253 30.472  1.00 79.64  ? 1007 GLU   D OE1 1 
ATOM   4589 O  OE2 . GLU   C 1 314 ? 46.878 -20.358 30.416  1.00 82.40  ? 1007 GLU   D OE2 1 
ATOM   4590 N  N   . GLU   C 1 315 ? 41.091 -18.145 30.617  1.00 62.70  ? 1008 GLU   D N   1 
ATOM   4591 C  CA  . GLU   C 1 315 ? 39.771 -18.530 30.122  1.00 60.26  ? 1008 GLU   D CA  1 
ATOM   4592 C  C   . GLU   C 1 315 ? 39.747 -20.008 29.698  1.00 57.41  ? 1008 GLU   D C   1 
ATOM   4593 O  O   . GLU   C 1 315 ? 40.797 -20.602 29.423  1.00 57.97  ? 1008 GLU   D O   1 
ATOM   4594 C  CB  . GLU   C 1 315 ? 39.359 -17.637 28.916  1.00 61.87  ? 1008 GLU   D CB  1 
ATOM   4595 C  CG  . GLU   C 1 315 ? 38.927 -16.208 29.238  1.00 63.97  ? 1008 GLU   D CG  1 
ATOM   4596 C  CD  . GLU   C 1 315 ? 37.519 -16.025 29.777  1.00 66.83  ? 1008 GLU   D CD  1 
ATOM   4597 O  OE1 . GLU   C 1 315 ? 36.850 -17.043 30.074  1.00 66.52  ? 1008 GLU   D OE1 1 
ATOM   4598 O  OE2 . GLU   C 1 315 ? 37.079 -14.858 29.901  1.00 68.10  ? 1008 GLU   D OE2 1 
ATOM   4599 N  N   . ASP   C 1 316 ? 38.556 -20.602 29.650  1.00 54.06  ? 1009 ASP   D N   1 
ATOM   4600 C  CA  . ASP   C 1 316 ? 38.407 -21.944 29.111  1.00 51.64  ? 1009 ASP   D CA  1 
ATOM   4601 C  C   . ASP   C 1 316 ? 38.124 -21.634 27.641  1.00 49.74  ? 1009 ASP   D C   1 
ATOM   4602 O  O   . ASP   C 1 316 ? 37.080 -21.062 27.385  1.00 50.13  ? 1009 ASP   D O   1 
ATOM   4603 C  CB  . ASP   C 1 316 ? 37.200 -22.655 29.758  1.00 51.59  ? 1009 ASP   D CB  1 
ATOM   4604 C  CG  . ASP   C 1 316 ? 36.916 -24.059 29.257  1.00 52.91  ? 1009 ASP   D CG  1 
ATOM   4605 O  OD1 . ASP   C 1 316 ? 37.662 -24.541 28.399  1.00 53.63  ? 1009 ASP   D OD1 1 
ATOM   4606 O  OD2 . ASP   C 1 316 ? 35.931 -24.662 29.710  1.00 54.21  ? 1009 ASP   D OD2 1 
ATOM   4607 N  N   . MET   C 1 317 ? 39.016 -21.959 26.679  1.00 47.66  ? 1010 MET   D N   1 
ATOM   4608 C  CA  . MET   C 1 317 ? 38.757 -21.648 25.261  1.00 46.33  ? 1010 MET   D CA  1 
ATOM   4609 C  C   . MET   C 1 317 ? 37.391 -22.169 24.743  1.00 45.53  ? 1010 MET   D C   1 
ATOM   4610 O  O   . MET   C 1 317 ? 36.818 -21.579 23.817  1.00 45.72  ? 1010 MET   D O   1 
ATOM   4611 C  CB  . MET   C 1 317 ? 39.910 -22.101 24.343  1.00 46.09  ? 1010 MET   D CB  1 
ATOM   4612 C  CG  . MET   C 1 317 ? 41.189 -21.350 24.605  1.00 46.75  ? 1010 MET   D CG  1 
ATOM   4613 S  SD  . MET   C 1 317 ? 42.506 -21.366 23.345  1.00 48.22  ? 1010 MET   D SD  1 
ATOM   4614 C  CE  . MET   C 1 317 ? 41.743 -20.385 22.059  1.00 45.05  ? 1010 MET   D CE  1 
ATOM   4615 N  N   . ASP   C 1 318 ? 36.852 -23.233 25.371  1.00 44.35  ? 1011 ASP   D N   1 
ATOM   4616 C  CA  . ASP   C 1 318 ? 35.549 -23.801 25.025  1.00 43.95  ? 1011 ASP   D CA  1 
ATOM   4617 C  C   . ASP   C 1 318 ? 34.369 -23.118 25.753  1.00 44.07  ? 1011 ASP   D C   1 
ATOM   4618 O  O   . ASP   C 1 318 ? 33.223 -23.223 25.321  1.00 44.08  ? 1011 ASP   D O   1 
ATOM   4619 C  CB  . ASP   C 1 318 ? 35.538 -25.306 25.298  1.00 44.96  ? 1011 ASP   D CB  1 
ATOM   4620 C  CG  . ASP   C 1 318 ? 34.319 -26.019 24.731  1.00 49.73  ? 1011 ASP   D CG  1 
ATOM   4621 O  OD1 . ASP   C 1 318 ? 33.983 -25.777 23.536  1.00 49.87  ? 1011 ASP   D OD1 1 
ATOM   4622 O  OD2 . ASP   C 1 318 ? 33.689 -26.815 25.481  1.00 52.28  ? 1011 ASP   D OD2 1 
ATOM   4623 N  N   . ASP   C 1 319 ? 34.643 -22.412 26.838  1.00 44.13  ? 1012 ASP   D N   1 
ATOM   4624 C  CA  . ASP   C 1 319 ? 33.626 -21.757 27.634  1.00 44.96  ? 1012 ASP   D CA  1 
ATOM   4625 C  C   . ASP   C 1 319 ? 34.143 -20.416 28.122  1.00 45.96  ? 1012 ASP   D C   1 
ATOM   4626 O  O   . ASP   C 1 319 ? 34.595 -20.291 29.260  1.00 45.93  ? 1012 ASP   D O   1 
ATOM   4627 C  CB  . ASP   C 1 319 ? 33.285 -22.654 28.822  1.00 46.08  ? 1012 ASP   D CB  1 
ATOM   4628 C  CG  . ASP   C 1 319 ? 31.871 -22.543 29.316  1.00 49.63  ? 1012 ASP   D CG  1 
ATOM   4629 O  OD1 . ASP   C 1 319 ? 31.199 -21.546 28.980  1.00 49.31  ? 1012 ASP   D OD1 1 
ATOM   4630 O  OD2 . ASP   C 1 319 ? 31.433 -23.453 30.027  1.00 53.04  ? 1012 ASP   D OD2 1 
ATOM   4631 N  N   . VAL   C 1 320 ? 34.117 -19.419 27.246  1.00 46.77  ? 1013 VAL   D N   1 
ATOM   4632 C  CA  . VAL   C 1 320 ? 34.606 -18.085 27.573  1.00 48.06  ? 1013 VAL   D CA  1 
ATOM   4633 C  C   . VAL   C 1 320 ? 33.506 -17.265 28.249  1.00 50.01  ? 1013 VAL   D C   1 
ATOM   4634 O  O   . VAL   C 1 320 ? 32.354 -17.345 27.835  1.00 50.17  ? 1013 VAL   D O   1 
ATOM   4635 C  CB  . VAL   C 1 320 ? 35.146 -17.413 26.301  1.00 48.18  ? 1013 VAL   D CB  1 
ATOM   4636 C  CG1 . VAL   C 1 320 ? 35.638 -16.012 26.588  1.00 48.78  ? 1013 VAL   D CG1 1 
ATOM   4637 C  CG2 . VAL   C 1 320 ? 36.254 -18.248 25.685  1.00 48.42  ? 1013 VAL   D CG2 1 
ATOM   4638 N  N   . VAL   C 1 321 ? 33.841 -16.510 29.301  1.00 51.55  ? 1014 VAL   D N   1 
ATOM   4639 C  CA  . VAL   C 1 321 ? 32.848 -15.728 30.016  1.00 53.90  ? 1014 VAL   D CA  1 
ATOM   4640 C  C   . VAL   C 1 321 ? 32.824 -14.269 29.557  1.00 56.77  ? 1014 VAL   D C   1 
ATOM   4641 O  O   . VAL   C 1 321 ? 31.735 -13.806 29.202  1.00 57.21  ? 1014 VAL   D O   1 
ATOM   4642 C  CB  . VAL   C 1 321 ? 32.947 -15.868 31.553  1.00 54.51  ? 1014 VAL   D CB  1 
ATOM   4643 C  CG1 . VAL   C 1 321 ? 34.353 -15.570 32.053  1.00 55.30  ? 1014 VAL   D CG1 1 
ATOM   4644 C  CG2 . VAL   C 1 321 ? 31.915 -14.998 32.257  1.00 54.77  ? 1014 VAL   D CG2 1 
ATOM   4645 N  N   . ASP   C 1 322 ? 33.976 -13.545 29.530  1.00 58.70  ? 1015 ASP   D N   1 
ATOM   4646 C  CA  . ASP   C 1 322 ? 33.982 -12.131 29.093  1.00 61.54  ? 1015 ASP   D CA  1 
ATOM   4647 C  C   . ASP   C 1 322 ? 33.328 -11.268 30.198  1.00 64.68  ? 1015 ASP   D C   1 
ATOM   4648 O  O   . ASP   C 1 322 ? 32.434 -10.467 29.920  1.00 64.60  ? 1015 ASP   D O   1 
ATOM   4649 C  CB  . ASP   C 1 322 ? 33.188 -12.004 27.768  1.00 62.89  ? 1015 ASP   D CB  1 
ATOM   4650 C  CG  . ASP   C 1 322 ? 33.425 -10.781 26.917  1.00 66.01  ? 1015 ASP   D CG  1 
ATOM   4651 O  OD1 . ASP   C 1 322 ? 34.550 -10.234 26.966  1.00 66.65  ? 1015 ASP   D OD1 1 
ATOM   4652 O  OD2 . ASP   C 1 322 ? 32.495 -10.392 26.170  1.00 67.25  ? 1015 ASP   D OD2 1 
ATOM   4653 N  N   . ALA   C 1 323 ? 33.754 -11.465 31.456  1.00 67.12  ? 1016 ALA   D N   1 
ATOM   4654 C  CA  . ALA   C 1 323 ? 33.140 -10.815 32.611  1.00 70.06  ? 1016 ALA   D CA  1 
ATOM   4655 C  C   . ALA   C 1 323 ? 33.421 -9.317  32.782  1.00 73.41  ? 1016 ALA   D C   1 
ATOM   4656 O  O   . ALA   C 1 323 ? 32.574 -8.608  33.341  1.00 73.86  ? 1016 ALA   D O   1 
ATOM   4657 C  CB  . ALA   C 1 323 ? 33.517 -11.554 33.886  1.00 70.04  ? 1016 ALA   D CB  1 
ATOM   4658 N  N   . ASP   C 1 324 ? 34.584 -8.828  32.313  1.00 75.47  ? 1017 ASP   D N   1 
ATOM   4659 C  CA  . ASP   C 1 324 ? 35.007 -7.432  32.496  1.00 77.88  ? 1017 ASP   D CA  1 
ATOM   4660 C  C   . ASP   C 1 324 ? 34.138 -6.364  31.836  1.00 80.41  ? 1017 ASP   D C   1 
ATOM   4661 O  O   . ASP   C 1 324 ? 34.424 -5.181  32.000  1.00 80.42  ? 1017 ASP   D O   1 
ATOM   4662 C  CB  . ASP   C 1 324 ? 36.455 -7.249  32.031  1.00 79.56  ? 1017 ASP   D CB  1 
ATOM   4663 C  CG  . ASP   C 1 324 ? 36.591 -7.263  30.525  1.00 83.99  ? 1017 ASP   D CG  1 
ATOM   4664 O  OD1 . ASP   C 1 324 ? 35.907 -8.089  29.877  1.00 84.58  ? 1017 ASP   D OD1 1 
ATOM   4665 O  OD2 . ASP   C 1 324 ? 37.344 -6.423  29.993  1.00 86.07  ? 1017 ASP   D OD2 1 
ATOM   4666 N  N   . GLU   C 1 325 ? 33.159 -6.764  31.025  1.00 82.48  ? 1018 GLU   D N   1 
ATOM   4667 C  CA  . GLU   C 1 325 ? 32.326 -5.807  30.317  1.00 85.01  ? 1018 GLU   D CA  1 
ATOM   4668 C  C   . GLU   C 1 325 ? 31.200 -5.261  31.175  1.00 87.44  ? 1018 GLU   D C   1 
ATOM   4669 O  O   . GLU   C 1 325 ? 30.700 -5.955  32.069  1.00 87.61  ? 1018 GLU   D O   1 
ATOM   4670 C  CB  . GLU   C 1 325 ? 31.793 -6.404  29.013  1.00 87.70  ? 1018 GLU   D CB  1 
ATOM   4671 C  CG  . GLU   C 1 325 ? 30.860 -7.583  29.217  1.00 93.07  ? 1018 GLU   D CG  1 
ATOM   4672 C  CD  . GLU   C 1 325 ? 30.171 -8.073  27.960  1.00 100.08 ? 1018 GLU   D CD  1 
ATOM   4673 O  OE1 . GLU   C 1 325 ? 30.586 -7.664  26.849  1.00 101.22 ? 1018 GLU   D OE1 1 
ATOM   4674 O  OE2 . GLU   C 1 325 ? 29.217 -8.875  28.086  1.00 102.58 ? 1018 GLU   D OE2 1 
ATOM   4675 N  N   . TYR   C 1 326 ? 30.830 -3.990  30.909  1.00 89.17  ? 1019 TYR   D N   1 
ATOM   4676 C  CA  . TYR   C 1 326 ? 29.764 -3.230  31.584  1.00 91.26  ? 1019 TYR   D CA  1 
ATOM   4677 C  C   . TYR   C 1 326 ? 29.490 -1.848  30.915  1.00 92.93  ? 1019 TYR   D C   1 
ATOM   4678 O  O   . TYR   C 1 326 ? 30.276 -1.408  30.067  1.00 92.94  ? 1019 TYR   D O   1 
ATOM   4679 C  CB  . TYR   C 1 326 ? 29.990 -3.092  33.116  1.00 91.32  ? 1019 TYR   D CB  1 
ATOM   4680 C  CG  . TYR   C 1 326 ? 31.427 -2.961  33.563  1.00 92.13  ? 1019 TYR   D CG  1 
ATOM   4681 C  CD1 . TYR   C 1 326 ? 32.206 -1.887  33.163  1.00 93.05  ? 1019 TYR   D CD1 1 
ATOM   4682 C  CD2 . TYR   C 1 326 ? 31.999 -3.901  34.403  1.00 93.17  ? 1019 TYR   D CD2 1 
ATOM   4683 C  CE1 . TYR   C 1 326 ? 33.527 -1.764  33.572  1.00 94.00  ? 1019 TYR   D CE1 1 
ATOM   4684 C  CE2 . TYR   C 1 326 ? 33.313 -3.783  34.831  1.00 94.12  ? 1019 TYR   D CE2 1 
ATOM   4685 C  CZ  . TYR   C 1 326 ? 34.079 -2.718  34.406  1.00 94.94  ? 1019 TYR   D CZ  1 
ATOM   4686 O  OH  . TYR   C 1 326 ? 35.380 -2.610  34.832  1.00 96.44  ? 1019 TYR   D OH  1 
ATOM   4687 N  N   . LEU   C 1 327 ? 28.346 -1.206  31.290  1.00 94.09  ? 1020 LEU   D N   1 
ATOM   4688 C  CA  . LEU   C 1 327 ? 27.844 0.101   30.831  1.00 95.79  ? 1020 LEU   D CA  1 
ATOM   4689 C  C   . LEU   C 1 327 ? 26.910 0.000   29.623  1.00 97.26  ? 1020 LEU   D C   1 
ATOM   4690 O  O   . LEU   C 1 327 ? 27.402 -0.171  28.502  1.00 97.70  ? 1020 LEU   D O   1 
ATOM   4691 C  CB  . LEU   C 1 327 ? 28.973 1.101   30.510  1.00 96.11  ? 1020 LEU   D CB  1 
ATOM   4692 C  CG  . LEU   C 1 327 ? 29.514 1.967   31.631  1.00 97.40  ? 1020 LEU   D CG  1 
ATOM   4693 C  CD1 . LEU   C 1 327 ? 30.717 1.317   32.277  1.00 97.87  ? 1020 LEU   D CD1 1 
ATOM   4694 C  CD2 . LEU   C 1 327 ? 29.941 3.301   31.082  1.00 98.06  ? 1020 LEU   D CD2 1 
ATOM   4695 N  N   . ILE   C 1 328 ? 25.575 0.148   29.835  1.00 97.68  ? 1021 ILE   D N   1 
ATOM   4696 C  CA  . ILE   C 1 328 ? 24.566 0.125   28.754  1.00 98.49  ? 1021 ILE   D CA  1 
ATOM   4697 C  C   . ILE   C 1 328 ? 23.216 0.701   29.220  1.00 98.69  ? 1021 ILE   D C   1 
ATOM   4698 O  O   . ILE   C 1 328 ? 22.544 1.420   28.476  1.00 98.63  ? 1021 ILE   D O   1 
ATOM   4699 C  CB  . ILE   C 1 328 ? 24.409 -1.269  28.070  1.00 99.28  ? 1021 ILE   D CB  1 
ATOM   4700 C  CG1 . ILE   C 1 328 ? 23.633 -1.168  26.738  1.00 100.39 ? 1021 ILE   D CG1 1 
ATOM   4701 C  CG2 . ILE   C 1 328 ? 23.814 -2.305  29.016  1.00 99.84  ? 1021 ILE   D CG2 1 
ATOM   4702 C  CD1 . ILE   C 1 328 ? 23.898 -2.316  25.770  1.00 101.70 ? 1021 ILE   D CD1 1 
HETATM 4703 C  C1  . A1IZ7 D 2 .   ? 21.083 -29.004 30.943  1.00 50.80  ? 1101 A1IZ7 A C1  1 
HETATM 4704 C  C2  . A1IZ7 D 2 .   ? 19.919 -29.496 31.501  1.00 51.38  ? 1101 A1IZ7 A C2  1 
HETATM 4705 C  C3  . A1IZ7 D 2 .   ? 19.987 -30.387 32.553  1.00 51.70  ? 1101 A1IZ7 A C3  1 
HETATM 4706 C  C7  . A1IZ7 D 2 .   ? 24.395 -33.345 35.048  1.00 47.81  ? 1101 A1IZ7 A C7  1 
HETATM 4707 C  C8  . A1IZ7 D 2 .   ? 24.606 -32.725 36.269  1.00 47.26  ? 1101 A1IZ7 A C8  1 
HETATM 4708 C  C9  . A1IZ7 D 2 .   ? 23.760 -31.703 36.697  1.00 46.85  ? 1101 A1IZ7 A C9  1 
HETATM 4709 C  C10 . A1IZ7 D 2 .   ? 22.666 -31.354 35.915  1.00 48.10  ? 1101 A1IZ7 A C10 1 
HETATM 4710 C  C11 . A1IZ7 D 2 .   ? 23.865 -31.099 38.032  1.00 45.21  ? 1101 A1IZ7 A C11 1 
HETATM 4711 C  C12 . A1IZ7 D 2 .   ? 23.283 -30.369 39.977  1.00 44.70  ? 1101 A1IZ7 A C12 1 
HETATM 4712 C  C13 . A1IZ7 D 2 .   ? 22.776 -29.810 41.288  1.00 44.96  ? 1101 A1IZ7 A C13 1 
HETATM 4713 C  C14 . A1IZ7 D 2 .   ? 25.191 -29.867 41.271  1.00 45.20  ? 1101 A1IZ7 A C14 1 
HETATM 4714 C  C15 . A1IZ7 D 2 .   ? 24.653 -30.355 39.971  1.00 44.79  ? 1101 A1IZ7 A C15 1 
HETATM 4715 C  C16 . A1IZ7 D 2 .   ? 26.418 -30.882 38.354  1.00 43.40  ? 1101 A1IZ7 A C16 1 
HETATM 4716 C  C19 . A1IZ7 D 2 .   ? 27.969 -30.315 36.823  1.00 42.76  ? 1101 A1IZ7 A C19 1 
HETATM 4717 C  C20 . A1IZ7 D 2 .   ? 24.059 -29.310 43.373  1.00 46.43  ? 1101 A1IZ7 A C20 1 
HETATM 4718 C  C21 . A1IZ7 D 2 .   ? 22.769 -28.989 44.105  1.00 46.80  ? 1101 A1IZ7 A C21 1 
HETATM 4719 C  C22 . A1IZ7 D 2 .   ? 22.951 -27.768 45.009  1.00 47.05  ? 1101 A1IZ7 A C22 1 
HETATM 4720 O  O1  . A1IZ7 D 2 .   ? 25.131 -29.202 43.946  1.00 46.72  ? 1101 A1IZ7 A O1  1 
HETATM 4721 N  N1  . A1IZ7 D 2 .   ? 23.993 -29.637 42.069  1.00 45.49  ? 1101 A1IZ7 A N1  1 
HETATM 4722 N  N   . A1IZ7 D 2 .   ? 22.803 -30.850 38.783  1.00 44.66  ? 1101 A1IZ7 A N   1 
HETATM 4723 N  N2  . A1IZ7 D 2 .   ? 25.027 -30.879 38.741  1.00 44.44  ? 1101 A1IZ7 A N2  1 
HETATM 4724 N  N4  . A1IZ7 D 2 .   ? 26.675 -30.373 37.147  1.00 43.17  ? 1101 A1IZ7 A N4  1 
HETATM 4725 N  N3  . A1IZ7 D 2 .   ? 29.012 -30.674 37.567  1.00 42.67  ? 1101 A1IZ7 A N3  1 
HETATM 4726 C  C18 . A1IZ7 D 2 .   ? 28.707 -31.097 38.798  1.00 42.52  ? 1101 A1IZ7 A C18 1 
HETATM 4727 C  C17 . A1IZ7 D 2 .   ? 27.412 -31.204 39.271  1.00 42.68  ? 1101 A1IZ7 A C17 1 
HETATM 4728 C  C6  . A1IZ7 D 2 .   ? 23.325 -32.972 34.250  1.00 48.54  ? 1101 A1IZ7 A C6  1 
HETATM 4729 C  C5  . A1IZ7 D 2 .   ? 22.499 -31.937 34.670  1.00 48.97  ? 1101 A1IZ7 A C5  1 
HETATM 4730 O  O   . A1IZ7 D 2 .   ? 21.305 -31.606 34.047  1.00 49.68  ? 1101 A1IZ7 A O   1 
HETATM 4731 C  C4  . A1IZ7 D 2 .   ? 21.268 -30.716 33.047  1.00 50.52  ? 1101 A1IZ7 A C4  1 
HETATM 4732 N  N5  . A1IZ7 D 2 .   ? 22.389 -30.255 32.533  1.00 50.44  ? 1101 A1IZ7 A N5  1 
HETATM 4733 C  C   . A1IZ7 D 2 .   ? 22.253 -29.424 31.525  1.00 50.32  ? 1101 A1IZ7 A C   1 
HETATM 4734 F  F   . A1IZ7 D 2 .   ? 23.424 -28.983 31.017  1.00 50.08  ? 1101 A1IZ7 A F   1 
HETATM 4735 CL CL  . A1IZ7 D 2 .   ? 18.523 -31.019 33.234  1.00 53.10  ? 1101 A1IZ7 A CL  1 
HETATM 4736 C  C1  . A1IZ7 E 2 .   ? 31.297 -3.309  16.388  1.00 50.60  ? 1101 A1IZ7 B C1  1 
HETATM 4737 C  C2  . A1IZ7 E 2 .   ? 31.263 -2.857  15.083  1.00 50.90  ? 1101 A1IZ7 B C2  1 
HETATM 4738 C  C3  . A1IZ7 E 2 .   ? 32.312 -2.108  14.590  1.00 51.18  ? 1101 A1IZ7 B C3  1 
HETATM 4739 C  C7  . A1IZ7 E 2 .   ? 36.948 0.467   17.035  1.00 50.45  ? 1101 A1IZ7 B C7  1 
HETATM 4740 C  C8  . A1IZ7 E 2 .   ? 38.039 -0.304  16.668  1.00 50.64  ? 1101 A1IZ7 B C8  1 
HETATM 4741 C  C9  . A1IZ7 E 2 .   ? 37.889 -1.355  15.775  1.00 50.81  ? 1101 A1IZ7 B C9  1 
HETATM 4742 C  C10 . A1IZ7 E 2 .   ? 36.644 -1.590  15.211  1.00 50.92  ? 1101 A1IZ7 B C10 1 
HETATM 4743 C  C11 . A1IZ7 E 2 .   ? 39.040 -2.134  15.291  1.00 51.25  ? 1101 A1IZ7 B C11 1 
HETATM 4744 C  C12 . A1IZ7 E 2 .   ? 40.409 -3.116  13.944  1.00 52.10  ? 1101 A1IZ7 B C12 1 
HETATM 4745 C  C13 . A1IZ7 E 2 .   ? 41.352 -3.825  12.998  1.00 52.65  ? 1101 A1IZ7 B C13 1 
HETATM 4746 C  C14 . A1IZ7 E 2 .   ? 42.353 -3.790  15.171  1.00 52.53  ? 1101 A1IZ7 B C14 1 
HETATM 4747 C  C15 . A1IZ7 E 2 .   ? 41.013 -3.144  15.168  1.00 52.02  ? 1101 A1IZ7 B C15 1 
HETATM 4748 C  C16 . A1IZ7 E 2 .   ? 40.474 -2.450  17.403  1.00 51.60  ? 1101 A1IZ7 B C16 1 
HETATM 4749 C  C19 . A1IZ7 E 2 .   ? 39.809 -2.882  19.501  1.00 51.91  ? 1101 A1IZ7 B C19 1 
HETATM 4750 C  C20 . A1IZ7 E 2 .   ? 43.740 -4.591  13.348  1.00 54.21  ? 1101 A1IZ7 B C20 1 
HETATM 4751 C  C21 . A1IZ7 E 2 .   ? 43.848 -4.987  11.920  1.00 53.11  ? 1101 A1IZ7 B C21 1 
HETATM 4752 C  C22 . A1IZ7 E 2 .   ? 44.548 -6.320  11.828  1.00 52.29  ? 1101 A1IZ7 B C22 1 
HETATM 4753 O  O1  . A1IZ7 E 2 .   ? 44.680 -4.790  14.113  1.00 55.59  ? 1101 A1IZ7 B O1  1 
HETATM 4754 N  N1  . A1IZ7 E 2 .   ? 42.556 -4.111  13.778  1.00 53.24  ? 1101 A1IZ7 B N1  1 
HETATM 4755 N  N   . A1IZ7 E 2 .   ? 39.187 -2.476  14.023  1.00 51.70  ? 1101 A1IZ7 B N   1 
HETATM 4756 N  N2  . A1IZ7 E 2 .   ? 40.171 -2.455  16.014  1.00 51.52  ? 1101 A1IZ7 B N2  1 
HETATM 4757 N  N4  . A1IZ7 E 2 .   ? 39.480 -2.806  18.213  1.00 51.69  ? 1101 A1IZ7 B N4  1 
HETATM 4758 N  N3  . A1IZ7 E 2 .   ? 41.006 -2.689  20.048  1.00 52.16  ? 1101 A1IZ7 B N3  1 
HETATM 4759 C  C18 . A1IZ7 E 2 .   ? 41.978 -2.395  19.184  1.00 52.08  ? 1101 A1IZ7 B C18 1 
HETATM 4760 C  C17 . A1IZ7 E 2 .   ? 41.772 -2.241  17.834  1.00 51.78  ? 1101 A1IZ7 B C17 1 
HETATM 4761 C  C6  . A1IZ7 E 2 .   ? 35.697 0.212   16.504  1.00 50.55  ? 1101 A1IZ7 B C6  1 
HETATM 4762 C  C5  . A1IZ7 E 2 .   ? 35.551 -0.843  15.623  1.00 51.06  ? 1101 A1IZ7 B C5  1 
HETATM 4763 O  O   . A1IZ7 E 2 .   ? 34.378 -1.079  14.923  1.00 51.41  ? 1101 A1IZ7 B O   1 
HETATM 4764 C  C4  . A1IZ7 E 2 .   ? 33.391 -1.853  15.439  1.00 51.23  ? 1101 A1IZ7 B C4  1 
HETATM 4765 N  N5  . A1IZ7 E 2 .   ? 33.451 -2.284  16.688  1.00 50.81  ? 1101 A1IZ7 B N5  1 
HETATM 4766 C  C   . A1IZ7 E 2 .   ? 32.425 -2.999  17.103  1.00 50.48  ? 1101 A1IZ7 B C   1 
HETATM 4767 F  F   . A1IZ7 E 2 .   ? 32.511 -3.400  18.390  1.00 50.53  ? 1101 A1IZ7 B F   1 
HETATM 4768 CL CL  . A1IZ7 E 2 .   ? 32.250 -1.546  12.957  1.00 51.41  ? 1101 A1IZ7 B CL  1 
HETATM 4769 O  O   . HOH   F 3 .   ? 30.956 -4.103  51.611  1.00 47.60  ? 1201 HOH   A O   1 
HETATM 4770 O  O   . HOH   F 3 .   ? 3.122  -15.163 35.277  1.00 40.20  ? 1202 HOH   A O   1 
HETATM 4771 O  O   . HOH   F 3 .   ? 3.273  -26.623 27.932  1.00 66.54  ? 1203 HOH   A O   1 
HETATM 4772 O  O   . HOH   F 3 .   ? 12.072 -44.311 34.146  1.00 47.98  ? 1204 HOH   A O   1 
HETATM 4773 O  O   . HOH   F 3 .   ? 15.842 -47.713 40.580  1.00 51.14  ? 1205 HOH   A O   1 
HETATM 4774 O  O   . HOH   F 3 .   ? 28.355 -40.390 21.428  1.00 53.47  ? 1206 HOH   A O   1 
HETATM 4775 O  O   . HOH   F 3 .   ? 18.070 -21.721 50.622  1.00 37.45  ? 1207 HOH   A O   1 
HETATM 4776 O  O   . HOH   F 3 .   ? 0.542  -21.904 49.624  1.00 53.80  ? 1208 HOH   A O   1 
HETATM 4777 O  O   . HOH   F 3 .   ? 18.111 -23.142 46.339  1.00 35.48  ? 1209 HOH   A O   1 
HETATM 4778 O  O   . HOH   F 3 .   ? -2.097 -20.139 51.851  1.00 33.20  ? 1210 HOH   A O   1 
HETATM 4779 O  O   . HOH   F 3 .   ? 8.782  -8.497  55.012  1.00 36.84  ? 1211 HOH   A O   1 
HETATM 4780 O  O   . HOH   F 3 .   ? 12.881 -26.840 35.470  1.00 40.87  ? 1212 HOH   A O   1 
HETATM 4781 O  O   . HOH   F 3 .   ? 0.389  -9.491  34.593  1.00 51.42  ? 1213 HOH   A O   1 
HETATM 4782 O  O   . HOH   F 3 .   ? 22.036 -12.363 27.972  1.00 29.15  ? 1214 HOH   A O   1 
HETATM 4783 O  O   . HOH   F 3 .   ? 18.858 -49.966 34.698  1.00 59.95  ? 1215 HOH   A O   1 
HETATM 4784 O  O   . HOH   F 3 .   ? 30.782 -6.731  35.945  1.00 56.27  ? 1216 HOH   A O   1 
HETATM 4785 O  O   . HOH   F 3 .   ? 23.144 -10.701 54.906  1.00 42.25  ? 1217 HOH   A O   1 
HETATM 4786 O  O   . HOH   F 3 .   ? 6.942  -26.789 36.949  1.00 47.42  ? 1218 HOH   A O   1 
HETATM 4787 O  O   . HOH   F 3 .   ? 7.068  -17.670 47.004  1.00 26.55  ? 1219 HOH   A O   1 
HETATM 4788 O  O   . HOH   F 3 .   ? 27.962 -28.597 46.155  1.00 48.34  ? 1220 HOH   A O   1 
HETATM 4789 O  O   . HOH   F 3 .   ? 35.608 -26.710 34.300  1.00 38.46  ? 1221 HOH   A O   1 
HETATM 4790 O  O   . HOH   F 3 .   ? 34.650 -16.671 47.262  1.00 44.11  ? 1222 HOH   A O   1 
HETATM 4791 O  O   . HOH   F 3 .   ? 12.030 -20.086 37.977  1.00 36.45  ? 1223 HOH   A O   1 
HETATM 4792 O  O   . HOH   F 3 .   ? 23.282 -5.677  26.172  1.00 44.12  ? 1224 HOH   A O   1 
HETATM 4793 O  O   . HOH   F 3 .   ? 8.348  -25.809 39.037  1.00 33.67  ? 1225 HOH   A O   1 
HETATM 4794 O  O   . HOH   F 3 .   ? 13.689 -44.475 30.183  1.00 34.41  ? 1226 HOH   A O   1 
HETATM 4795 O  O   . HOH   F 3 .   ? 26.377 -32.987 18.565  1.00 42.07  ? 1227 HOH   A O   1 
HETATM 4796 O  O   . HOH   F 3 .   ? 31.405 -48.035 30.568  1.00 46.05  ? 1228 HOH   A O   1 
HETATM 4797 O  O   . HOH   F 3 .   ? 14.828 -9.711  29.526  1.00 55.41  ? 1229 HOH   A O   1 
HETATM 4798 O  O   . HOH   F 3 .   ? 13.191 -17.146 31.401  1.00 46.07  ? 1230 HOH   A O   1 
HETATM 4799 O  O   . HOH   F 3 .   ? 25.560 -12.919 27.591  1.00 29.86  ? 1231 HOH   A O   1 
HETATM 4800 O  O   . HOH   F 3 .   ? 15.552 -29.252 39.498  1.00 45.40  ? 1232 HOH   A O   1 
HETATM 4801 O  O   . HOH   F 3 .   ? 39.856 -3.138  53.180  1.00 57.94  ? 1233 HOH   A O   1 
HETATM 4802 O  O   . HOH   F 3 .   ? 17.746 -32.330 40.048  1.00 54.21  ? 1234 HOH   A O   1 
HETATM 4803 O  O   . HOH   F 3 .   ? 16.855 0.149   43.078  1.00 48.00  ? 1235 HOH   A O   1 
HETATM 4804 O  O   . HOH   F 3 .   ? 19.743 -42.490 41.310  1.00 40.20  ? 1236 HOH   A O   1 
HETATM 4805 O  O   . HOH   F 3 .   ? 16.925 -24.965 48.041  1.00 32.34  ? 1237 HOH   A O   1 
HETATM 4806 O  O   . HOH   F 3 .   ? 17.892 -28.937 42.493  1.00 52.84  ? 1238 HOH   A O   1 
HETATM 4807 O  O   . HOH   F 3 .   ? 24.348 -22.719 26.613  1.00 58.11  ? 1239 HOH   A O   1 
HETATM 4808 O  O   . HOH   F 3 .   ? 6.828  -19.358 39.632  1.00 55.30  ? 1240 HOH   A O   1 
HETATM 4809 O  O   . HOH   F 3 .   ? 20.245 1.512   52.892  1.00 53.85  ? 1241 HOH   A O   1 
HETATM 4810 O  O   . HOH   F 3 .   ? 9.535  -2.875  38.701  1.00 49.86  ? 1242 HOH   A O   1 
HETATM 4811 O  O   . HOH   F 3 .   ? 16.037 -44.355 40.930  1.00 39.58  ? 1243 HOH   A O   1 
HETATM 4812 O  O   . HOH   F 3 .   ? 11.844 -22.484 41.790  1.00 23.07  ? 1244 HOH   A O   1 
HETATM 4813 O  O   . HOH   F 3 .   ? 26.139 -40.123 20.076  1.00 42.26  ? 1245 HOH   A O   1 
HETATM 4814 O  O   . HOH   F 3 .   ? 23.733 -34.791 48.716  1.00 68.32  ? 1246 HOH   A O   1 
HETATM 4815 O  O   . HOH   F 3 .   ? -1.443 -12.308 60.638  1.00 49.59  ? 1247 HOH   A O   1 
HETATM 4816 O  O   . HOH   F 3 .   ? 8.863  -22.640 27.760  1.00 41.76  ? 1248 HOH   A O   1 
HETATM 4817 O  O   . HOH   F 3 .   ? -4.833 -13.874 53.240  1.00 58.11  ? 1249 HOH   A O   1 
HETATM 4818 O  O   . HOH   F 3 .   ? 5.982  -27.013 54.808  1.00 55.82  ? 1250 HOH   A O   1 
HETATM 4819 O  O   . HOH   F 3 .   ? 35.023 -10.194 52.178  1.00 38.39  ? 1251 HOH   A O   1 
HETATM 4820 O  O   . HOH   F 3 .   ? 26.400 -6.071  57.626  1.00 53.16  ? 1252 HOH   A O   1 
HETATM 4821 O  O   . HOH   F 3 .   ? 23.816 -39.758 18.773  1.00 40.51  ? 1253 HOH   A O   1 
HETATM 4822 O  O   . HOH   F 3 .   ? 26.661 2.396   51.643  1.00 39.12  ? 1254 HOH   A O   1 
HETATM 4823 O  O   . HOH   F 3 .   ? 2.411  -27.450 54.051  1.00 36.11  ? 1255 HOH   A O   1 
HETATM 4824 O  O   . HOH   F 3 .   ? 27.209 -23.194 19.628  1.00 40.43  ? 1256 HOH   A O   1 
HETATM 4825 O  O   . HOH   F 3 .   ? 31.686 -25.276 47.290  1.00 57.99  ? 1257 HOH   A O   1 
HETATM 4826 O  O   . HOH   F 3 .   ? 21.402 -34.293 16.659  1.00 61.78  ? 1258 HOH   A O   1 
HETATM 4827 O  O   . HOH   F 3 .   ? 24.686 -38.867 48.592  1.00 57.56  ? 1259 HOH   A O   1 
HETATM 4828 O  O   . HOH   F 3 .   ? 25.580 -46.452 32.868  1.00 43.16  ? 1260 HOH   A O   1 
HETATM 4829 O  O   . HOH   F 3 .   ? 14.623 -48.384 27.134  1.00 49.36  ? 1261 HOH   A O   1 
HETATM 4830 O  O   . HOH   F 3 .   ? -3.875 -14.988 57.099  1.00 61.04  ? 1262 HOH   A O   1 
HETATM 4831 O  O   . HOH   F 3 .   ? 15.172 -10.724 25.907  1.00 28.22  ? 1263 HOH   A O   1 
HETATM 4832 O  O   . HOH   F 3 .   ? 31.978 3.246   48.170  1.00 44.60  ? 1264 HOH   A O   1 
HETATM 4833 O  O   . HOH   F 3 .   ? 20.868 -45.210 24.423  1.00 40.78  ? 1265 HOH   A O   1 
HETATM 4834 O  O   . HOH   F 3 .   ? 33.908 -11.352 39.836  1.00 59.07  ? 1266 HOH   A O   1 
HETATM 4835 O  O   . HOH   F 3 .   ? 36.229 -38.035 36.913  1.00 52.26  ? 1267 HOH   A O   1 
HETATM 4836 O  O   . HOH   F 3 .   ? 17.985 -33.573 42.295  1.00 63.18  ? 1268 HOH   A O   1 
HETATM 4837 O  O   . HOH   F 3 .   ? 8.725  -44.457 22.593  1.00 36.33  ? 1269 HOH   A O   1 
HETATM 4838 O  O   . HOH   F 3 .   ? 21.456 2.314   35.844  1.00 50.35  ? 1270 HOH   A O   1 
HETATM 4839 O  O   . HOH   F 3 .   ? 21.833 -47.504 34.657  1.00 46.34  ? 1271 HOH   A O   1 
HETATM 4840 O  O   . HOH   F 3 .   ? 11.536 -43.392 48.305  1.00 37.87  ? 1272 HOH   A O   1 
HETATM 4841 O  O   . HOH   F 3 .   ? 23.573 3.504   48.032  1.00 56.28  ? 1273 HOH   A O   1 
HETATM 4842 O  O   . HOH   F 3 .   ? 18.093 -15.123 57.413  1.00 37.13  ? 1274 HOH   A O   1 
HETATM 4843 O  O   . HOH   F 3 .   ? 20.787 1.933   42.622  1.00 49.00  ? 1275 HOH   A O   1 
HETATM 4844 O  O   . HOH   F 3 .   ? 24.826 -32.591 44.151  1.00 42.07  ? 1276 HOH   A O   1 
HETATM 4845 O  O   . HOH   F 3 .   ? 32.026 -22.281 57.012  1.00 62.72  ? 1277 HOH   A O   1 
HETATM 4846 O  O   . HOH   F 3 .   ? 29.319 -26.486 30.575  1.00 39.03  ? 1278 HOH   A O   1 
HETATM 4847 O  O   . HOH   F 3 .   ? 11.934 -6.394  55.682  1.00 40.47  ? 1279 HOH   A O   1 
HETATM 4848 O  O   . HOH   F 3 .   ? 21.908 -32.980 43.910  1.00 45.38  ? 1280 HOH   A O   1 
HETATM 4849 O  O   . HOH   F 3 .   ? 13.274 -41.436 34.551  1.00 38.21  ? 1281 HOH   A O   1 
HETATM 4850 O  O   . HOH   F 3 .   ? 13.835 -17.745 19.279  1.00 44.12  ? 1282 HOH   A O   1 
HETATM 4851 O  O   . HOH   F 3 .   ? 18.095 -22.722 17.744  1.00 55.89  ? 1283 HOH   A O   1 
HETATM 4852 O  O   . HOH   F 3 .   ? 5.763  -15.248 28.771  1.00 44.52  ? 1284 HOH   A O   1 
HETATM 4853 O  O   . HOH   F 3 .   ? 23.891 -28.403 20.054  1.00 45.68  ? 1285 HOH   A O   1 
HETATM 4854 O  O   . HOH   F 3 .   ? 16.221 -9.590  21.757  1.00 44.53  ? 1286 HOH   A O   1 
HETATM 4855 O  O   . HOH   F 3 .   ? 29.070 -19.549 22.715  1.00 47.04  ? 1287 HOH   A O   1 
HETATM 4856 O  O   . HOH   F 3 .   ? 9.341  -2.580  34.743  1.00 51.55  ? 1288 HOH   A O   1 
HETATM 4857 O  O   . HOH   F 3 .   ? -1.868 -19.152 57.147  1.00 58.89  ? 1289 HOH   A O   1 
HETATM 4858 O  O   . HOH   F 3 .   ? 1.179  -28.692 46.081  1.00 41.75  ? 1290 HOH   A O   1 
HETATM 4859 O  O   . HOH   F 3 .   ? 12.474 -29.086 46.429  1.00 45.44  ? 1291 HOH   A O   1 
HETATM 4860 O  O   . HOH   F 3 .   ? 23.186 -1.744  55.504  1.00 44.11  ? 1292 HOH   A O   1 
HETATM 4861 O  O   . HOH   F 3 .   ? 13.423 -23.565 52.110  1.00 51.90  ? 1293 HOH   A O   1 
HETATM 4862 O  O   . HOH   F 3 .   ? 10.963 -27.461 47.778  1.00 41.23  ? 1294 HOH   A O   1 
HETATM 4863 O  O   . HOH   F 3 .   ? 23.276 -31.637 46.497  1.00 51.50  ? 1295 HOH   A O   1 
HETATM 4864 O  O   . HOH   F 3 .   ? 9.243  -25.330 49.638  1.00 17.78  ? 1296 HOH   A O   1 
HETATM 4865 O  O   . HOH   F 3 .   ? 16.606 -23.966 50.914  1.00 42.09  ? 1297 HOH   A O   1 
HETATM 4866 O  O   . HOH   F 3 .   ? 1.322  -13.608 33.839  1.00 36.26  ? 1298 HOH   A O   1 
HETATM 4867 O  O   . HOH   F 3 .   ? 5.345  -44.093 29.842  1.00 57.62  ? 1299 HOH   A O   1 
HETATM 4868 O  O   . HOH   F 3 .   ? 18.236 -12.093 56.832  1.00 43.86  ? 1300 HOH   A O   1 
HETATM 4869 O  O   . HOH   F 3 .   ? 18.854 -47.055 40.121  1.00 49.41  ? 1301 HOH   A O   1 
HETATM 4870 O  O   . HOH   F 3 .   ? 14.022 -4.719  27.907  1.00 46.07  ? 1302 HOH   A O   1 
HETATM 4871 O  O   . HOH   F 3 .   ? 19.872 -30.821 44.595  1.00 52.56  ? 1303 HOH   A O   1 
HETATM 4872 O  O   . HOH   F 3 .   ? 13.716 -7.494  27.564  1.00 56.68  ? 1304 HOH   A O   1 
HETATM 4873 O  O   . HOH   F 3 .   ? -3.696 -20.686 56.328  1.00 53.29  ? 1305 HOH   A O   1 
HETATM 4874 O  O   . HOH   G 3 .   ? 38.217 15.508  5.672   1.00 39.27  ? 1201 HOH   B O   1 
HETATM 4875 O  O   . HOH   G 3 .   ? 50.653 -24.416 7.840   1.00 38.79  ? 1202 HOH   B O   1 
HETATM 4876 O  O   . HOH   G 3 .   ? 39.973 -20.727 -2.234  1.00 32.64  ? 1203 HOH   B O   1 
HETATM 4877 O  O   . HOH   G 3 .   ? 29.449 -12.491 3.182   1.00 25.74  ? 1204 HOH   B O   1 
HETATM 4878 O  O   . HOH   G 3 .   ? 38.026 15.402  24.142  1.00 59.62  ? 1205 HOH   B O   1 
HETATM 4879 O  O   . HOH   G 3 .   ? 33.899 -24.243 -11.973 1.00 27.56  ? 1206 HOH   B O   1 
HETATM 4880 O  O   . HOH   G 3 .   ? 31.080 -5.779  7.512   1.00 37.00  ? 1207 HOH   B O   1 
HETATM 4881 O  O   . HOH   G 3 .   ? 26.643 -14.562 9.017   1.00 23.59  ? 1208 HOH   B O   1 
HETATM 4882 O  O   . HOH   G 3 .   ? 41.360 9.722   11.008  1.00 35.15  ? 1209 HOH   B O   1 
HETATM 4883 O  O   . HOH   G 3 .   ? 33.021 11.997  14.585  1.00 39.06  ? 1210 HOH   B O   1 
HETATM 4884 O  O   . HOH   G 3 .   ? 34.316 -7.170  26.653  1.00 48.56  ? 1211 HOH   B O   1 
HETATM 4885 O  O   . HOH   G 3 .   ? 45.434 -9.229  -15.611 1.00 46.45  ? 1212 HOH   B O   1 
HETATM 4886 O  O   . HOH   G 3 .   ? 48.985 -10.454 -2.542  1.00 51.15  ? 1213 HOH   B O   1 
HETATM 4887 O  O   . HOH   G 3 .   ? 47.300 -5.893  15.607  1.00 45.83  ? 1214 HOH   B O   1 
HETATM 4888 O  O   . HOH   G 3 .   ? 25.839 -21.126 7.996   1.00 36.57  ? 1215 HOH   B O   1 
HETATM 4889 O  O   . HOH   G 3 .   ? 42.973 -10.733 6.959   1.00 33.54  ? 1216 HOH   B O   1 
HETATM 4890 O  O   . HOH   G 3 .   ? 43.492 -37.112 10.476  1.00 53.19  ? 1217 HOH   B O   1 
HETATM 4891 O  O   . HOH   G 3 .   ? 36.468 -32.868 7.231   1.00 54.18  ? 1218 HOH   B O   1 
HETATM 4892 O  O   . HOH   G 3 .   ? 38.426 -27.604 -7.395  1.00 45.18  ? 1219 HOH   B O   1 
HETATM 4893 O  O   . HOH   G 3 .   ? 32.838 -6.172  2.205   1.00 41.08  ? 1220 HOH   B O   1 
HETATM 4894 O  O   . HOH   G 3 .   ? 32.272 -31.791 18.705  1.00 43.02  ? 1221 HOH   B O   1 
HETATM 4895 O  O   . HOH   G 3 .   ? 32.238 -12.389 5.293   1.00 38.64  ? 1222 HOH   B O   1 
HETATM 4896 O  O   . HOH   G 3 .   ? 34.390 -14.456 -14.739 1.00 44.97  ? 1223 HOH   B O   1 
HETATM 4897 O  O   . HOH   G 3 .   ? 33.379 -3.102  23.582  1.00 55.42  ? 1224 HOH   B O   1 
HETATM 4898 O  O   . HOH   G 3 .   ? 22.485 -7.307  0.611   1.00 64.25  ? 1225 HOH   B O   1 
HETATM 4899 O  O   . HOH   G 3 .   ? 26.638 8.977   31.399  1.00 60.39  ? 1226 HOH   B O   1 
HETATM 4900 O  O   . HOH   G 3 .   ? 43.944 -8.820  5.377   1.00 28.51  ? 1227 HOH   B O   1 
HETATM 4901 O  O   . HOH   G 3 .   ? 46.832 -11.232 -1.282  1.00 54.27  ? 1228 HOH   B O   1 
HETATM 4902 O  O   . HOH   G 3 .   ? 24.729 -22.164 11.500  1.00 41.06  ? 1229 HOH   B O   1 
HETATM 4903 O  O   . HOH   G 3 .   ? 22.840 -9.505  -1.240  1.00 48.72  ? 1230 HOH   B O   1 
HETATM 4904 O  O   . HOH   G 3 .   ? 54.491 -25.109 19.858  1.00 38.85  ? 1231 HOH   B O   1 
HETATM 4905 O  O   . HOH   G 3 .   ? 45.747 -2.943  16.158  1.00 64.52  ? 1232 HOH   B O   1 
HETATM 4906 O  O   . HOH   G 3 .   ? 33.916 -6.915  -8.354  1.00 57.07  ? 1233 HOH   B O   1 
HETATM 4907 O  O   . HOH   G 3 .   ? 19.570 -8.860  18.590  1.00 56.89  ? 1234 HOH   B O   1 
HETATM 4908 O  O   . HOH   G 3 .   ? 52.556 -14.768 2.074   1.00 38.62  ? 1235 HOH   B O   1 
HETATM 4909 O  O   . HOH   G 3 .   ? 30.918 -9.203  23.843  1.00 44.69  ? 1236 HOH   B O   1 
HETATM 4910 O  O   . HOH   G 3 .   ? 27.977 12.524  18.106  1.00 52.04  ? 1237 HOH   B O   1 
HETATM 4911 O  O   . HOH   G 3 .   ? 31.138 10.996  6.362   1.00 39.08  ? 1238 HOH   B O   1 
HETATM 4912 O  O   . HOH   G 3 .   ? 29.155 11.617  9.528   1.00 50.99  ? 1239 HOH   B O   1 
HETATM 4913 O  O   . HOH   G 3 .   ? 28.039 -7.688  20.839  1.00 53.20  ? 1240 HOH   B O   1 
HETATM 4914 O  O   . HOH   G 3 .   ? 28.008 -9.744  22.000  1.00 35.38  ? 1241 HOH   B O   1 
HETATM 4915 O  O   . HOH   G 3 .   ? 49.798 -8.904  17.590  1.00 36.64  ? 1242 HOH   B O   1 
HETATM 4916 O  O   . HOH   G 3 .   ? 16.190 8.176   9.275   1.00 57.93  ? 1243 HOH   B O   1 
HETATM 4917 O  O   . HOH   G 3 .   ? 39.869 1.196   8.412   1.00 39.35  ? 1244 HOH   B O   1 
HETATM 4918 O  O   . HOH   G 3 .   ? 45.004 -6.282  -12.846 1.00 53.73  ? 1245 HOH   B O   1 
HETATM 4919 O  O   . HOH   G 3 .   ? 53.117 -20.736 5.682   1.00 53.24  ? 1246 HOH   B O   1 
HETATM 4920 O  O   . HOH   G 3 .   ? 26.980 -5.800  6.931   1.00 57.65  ? 1247 HOH   B O   1 
HETATM 4921 O  O   . HOH   G 3 .   ? 32.481 9.037   7.759   1.00 42.24  ? 1248 HOH   B O   1 
HETATM 4922 O  O   . HOH   G 3 .   ? 32.593 6.263   37.603  1.00 70.27  ? 1249 HOH   B O   1 
HETATM 4923 O  O   . HOH   G 3 .   ? 20.468 -7.300  3.212   1.00 71.35  ? 1250 HOH   B O   1 
HETATM 4924 O  O   . HOH   G 3 .   ? 38.019 15.545  8.673   1.00 33.56  ? 1251 HOH   B O   1 
HETATM 4925 O  O   . HOH   G 3 .   ? 39.728 -27.823 23.843  1.00 48.01  ? 1252 HOH   B O   1 
HETATM 4926 O  O   . HOH   G 3 .   ? 33.226 -4.108  6.838   1.00 64.70  ? 1253 HOH   B O   1 
HETATM 4927 O  O   . HOH   G 3 .   ? 53.575 -16.946 7.044   1.00 67.67  ? 1254 HOH   B O   1 
HETATM 4928 O  O   . HOH   G 3 .   ? 34.567 -3.276  -7.386  1.00 73.63  ? 1255 HOH   B O   1 
HETATM 4929 O  O   . HOH   G 3 .   ? 36.338 14.883  13.959  1.00 40.64  ? 1256 HOH   B O   1 
HETATM 4930 O  O   . HOH   G 3 .   ? 42.558 7.837   6.940   1.00 57.42  ? 1257 HOH   B O   1 
HETATM 4931 O  O   . HOH   G 3 .   ? 29.341 -2.980  27.083  1.00 47.48  ? 1258 HOH   B O   1 
HETATM 4932 O  O   . HOH   G 3 .   ? 44.978 -30.833 -1.683  1.00 36.12  ? 1259 HOH   B O   1 
HETATM 4933 O  O   . HOH   G 3 .   ? 21.899 -21.262 13.672  1.00 43.36  ? 1260 HOH   B O   1 
HETATM 4934 O  O   . HOH   G 3 .   ? 38.166 -36.294 6.750   1.00 58.51  ? 1261 HOH   B O   1 
HETATM 4935 O  O   . HOH   G 3 .   ? 21.806 -8.096  27.214  1.00 46.16  ? 1262 HOH   B O   1 
HETATM 4936 O  O   . HOH   G 3 .   ? 33.098 -20.085 24.202  1.00 29.83  ? 1263 HOH   B O   1 
HETATM 4937 O  O   . HOH   G 3 .   ? 41.970 12.568  14.355  1.00 46.35  ? 1264 HOH   B O   1 
HETATM 4938 O  O   . HOH   G 3 .   ? 49.941 -32.930 7.481   1.00 50.34  ? 1265 HOH   B O   1 
HETATM 4939 O  O   . HOH   G 3 .   ? 27.564 -29.910 4.793   1.00 31.87  ? 1266 HOH   B O   1 
HETATM 4940 O  O   . HOH   G 3 .   ? 22.482 -7.738  7.388   1.00 32.45  ? 1267 HOH   B O   1 
HETATM 4941 O  O   . HOH   G 3 .   ? 17.424 -9.174  8.635   1.00 51.50  ? 1268 HOH   B O   1 
HETATM 4942 O  O   . HOH   G 3 .   ? 25.180 -28.715 4.944   1.00 49.05  ? 1269 HOH   B O   1 
HETATM 4943 O  O   . HOH   G 3 .   ? 43.355 -5.950  -9.920  1.00 53.56  ? 1270 HOH   B O   1 
HETATM 4944 O  O   . HOH   G 3 .   ? 50.594 0.590   16.955  1.00 52.16  ? 1271 HOH   B O   1 
HETATM 4945 O  O   . HOH   G 3 .   ? 34.737 -5.569  22.592  1.00 48.18  ? 1272 HOH   B O   1 
HETATM 4946 O  O   . HOH   G 3 .   ? 40.644 8.751   8.724   1.00 38.96  ? 1273 HOH   B O   1 
HETATM 4947 O  O   . HOH   G 3 .   ? 53.630 -11.538 5.504   1.00 47.42  ? 1274 HOH   B O   1 
HETATM 4948 O  O   . HOH   G 3 .   ? 47.939 3.087   4.435   1.00 56.12  ? 1275 HOH   B O   1 
HETATM 4949 O  O   . HOH   G 3 .   ? 48.632 -25.188 21.564  1.00 50.61  ? 1276 HOH   B O   1 
HETATM 4950 O  O   . HOH   G 3 .   ? 15.997 -14.224 16.225  1.00 43.96  ? 1277 HOH   B O   1 
HETATM 4951 O  O   . HOH   G 3 .   ? 21.247 -14.606 4.069   1.00 42.11  ? 1278 HOH   B O   1 
HETATM 4952 O  O   . HOH   G 3 .   ? 44.566 -1.065  13.605  1.00 52.76  ? 1279 HOH   B O   1 
HETATM 4953 O  O   . HOH   G 3 .   ? 26.305 14.759  21.318  1.00 59.10  ? 1280 HOH   B O   1 
HETATM 4954 O  O   . HOH   G 3 .   ? 46.355 -11.004 4.291   1.00 39.60  ? 1281 HOH   B O   1 
HETATM 4955 O  O   . HOH   G 3 .   ? 53.094 -8.992  4.953   1.00 56.70  ? 1282 HOH   B O   1 
HETATM 4956 O  O   . HOH   G 3 .   ? 22.278 -23.951 10.757  1.00 45.24  ? 1283 HOH   B O   1 
HETATM 4957 O  O   . HOH   G 3 .   ? 8.635  0.702   17.406  1.00 72.01  ? 1284 HOH   B O   1 
HETATM 4958 O  O   . HOH   G 3 .   ? 7.086  -2.779  17.513  1.00 54.50  ? 1285 HOH   B O   1 
HETATM 4959 O  O   . HOH   H 3 .   ? 36.293 -19.505 31.079  1.00 47.19  ? 1101 HOH   D O   1 
HETATM 4960 O  O   . HOH   H 3 .   ? 42.199 -15.785 29.424  1.00 52.05  ? 1102 HOH   D O   1 
HETATM 4961 O  O   . HOH   H 3 .   ? 41.971 -19.923 35.775  1.00 64.93  ? 1103 HOH   D O   1 
HETATM 4962 O  O   . HOH   H 3 .   ? 39.631 -26.071 25.845  1.00 39.27  ? 1104 HOH   D O   1 
HETATM 4963 O  O   . HOH   H 3 .   ? 28.224 -12.372 26.618  1.00 34.99  ? 1105 HOH   D O   1 
# 
